U.S. Department of Energy

Pacific Northwest National Laboratory

Garry Buchko

Garry Buchko
Professional Title: 
Scientist
Phone Number: 
(509) 371-6543
Email: 
garry.buchko@pnnl.gov
Biography: 

Dr. Garry W. Buchko is a physical biochemist that first joined PNNL as a postdoctoral fellow with Dr. Michael Kennedy in 1995 and was promoted to senior scientist in 2001. In 2017 he accepted a joint-appointment as an Associate Professor with the School of Molecular Biosciences at Washington State University. He received his M.Sc. in Chemistry at McMaster University (1986) under the supervision of Drs. Russell Bell and the late Tom Nelson, pioneers in the field of ribonucleic acid synthetic chemistry. This was followed by a doctorate degree in Chemistry at the University of Manitoba (1989) with Dr. Frank Hruska, a pioneer in using NMR spectroscopy to study nucleic acid sugar conformations. His first two postdoctoral experiences were with the radiation biologists Drs. Jean Cadet in Grenoble, France (Laboratoire des Lesions des Acides Nucléique, Centre d'Etudes Nucléaires de Grenoble) and Michael Weinfeld in Edmonton, Alberta (Cross Cancer Institute). His third postdoctoral experience was with the NMR spectroscopist/protein biochemist Dr. Bob Cushley in Burnaby, British Columbia (Institute of Molecular Biology and Biochemistry, Simon Fraser University). Currently, Dr. Buchko is the PNNL-WSU component of the Seattle Structural Genomics Center for Infectious Disease (SSGCID, www.ssgcid.org), a consortium of researchers at Seattle Children's (formerly the Center for Infectious Disease Research), UCB (formerly Beryllium), and the University of Washington. SSGCID is funded by the National Institute of Allergies and Infectious Diseases (NIAID) and devoted to applying state-of-the-art structural genomics technologies to structurally characterize targeted proteins from NIAID Category A-C pathogens and organisms. In addition to the SSGCID structural biology efforts, Dr. Buchko is also part of a team of PNNL scientists, lead by Dr. Wendy Shaw and funded by National Institute of Dental and Craniofacial Research, studying amelogenin's role in the formation of tooth enamel (biomineralization).

Education: 
  • Ph.D., Chemistry, University of Manitoba (1989)
  • M.Sc., Chemistry, McMaster University (1986)
  • B.Sc.(Hons), Biochemistry, University of Manitoba (1983)
Awards: 
  • Outstanding Performance Award, Catalysis Science Group, PNNL, 2015
  • Outstanding Performance Award, Biomineralization, PNNL, 2010,
  • Outstanding Performance Award, EMSL Molecular Biology Grand Challenge, PNNL, 2008
  • International Workshop on Radiation Damage in DNA Travel Award, 1994
  • BC and Yukon Heart & Stroke Research Fellowship, 1993-1995
  • Alberta Cancer Board Research Fellowship, 1991-1992
  • American Association of Cancer Research Travel Award, 1991
  • Government of France, France-Canada Postdoctoral Fellowship, 1990
  • A.N. Campbell Travel Award, 1989
Research Interests: 

Advancing infectious disease research through structural genomics:  The NMR component of the Seattle Structural Genomics Center for Infectious Diseases (SSGCID)

Since 2007 a major part of my research has been associated with the Seattle Structural Genomics Center for Infectious Disease (http://ssgcid.org), one of two Structural Genomics centers established by NIAID to solve protein structures from organisms causing infectious disease. Both Centers actively engage with infectious disease researchers to select Community Request (CR) targets for entry in their structure determination pipelines and to collaboratively interpret and publish results from successful structure determinations. SSGCID target selection focuses on essential enzymes, virulence factors, drug targets and vaccine candidates from numerous bacterial, eukaryotic, viral pathogens. In general, target genes are PCR amplified, cloned and screened for soluble expression in Escherichia coli. Proteins are then purified in milligram amounts, screened for crystallization, and analyzed by X-ray diffraction using an in-house source or off-site synchrotron beam-line.  Proteins <25 kDa in molecular weight that fail to crystallize are queued for structure determination by NMR. In 2018 cryo-EM was added to our suite of structure determination capabilities. Since project inception in late 2007, over 6,000 targets have entered the SSGCID structure determination pipeline, of which >4000 are CRs, resulting in deposition of nearly 1,200 protein structures in the Protein Data Bank (PDB). In addition, more than 8000 expression clones and 4000 purified proteins are publicly available free of charge. Target-to-structure success rates vary considerably between genera (1-17%) and about one third of all SSGCID structures contain bound ligands. Each year ~25-50 High Value Targets (HVTs) from CRs enter several rescue pathways, including protein truncation or mutagenesis, selection of orthologues from related species, and use of yeast, baculovirus and/or mammalian expression systems. In addition to the CR target pipeline, SSGCID has initiated >60 Community Research Projects (CRPs) with collaborators from the scientific community and from these undertake 3 Functional (FUN) studies each year using structural data to guide hypothesis-driven experimental approaches aimed at elucidating the function of selected targets.  New targets and new functional studies are continuously being solicited.  Please visit our website or contact me if your research would benefit from structural data. 


Repairing dental enamel – A multipronged approach to identify structural features guiding enamel formation

Most of us have visited a dentist in our lifetime due to damage to the 1-2 nm layer of enamel on the surface of our teeth. If we could understand the molecular mechanism of the biomineralization process that generates enamel in vivo it may be possible to repair or regenerate enamel more efficiently.

Magnified view (upper right) showing the intricate structure of dental enamel. Crystal growth is guided by the protein amelogeninbound to the solid HAP surface (bottom). The molecular mechanism is poorly understood.

Made of ~95 mineral by weight, tooth enamel is one of nature’s hardest tissues. The exceptional strength and robust mechanical properties of enamel arise from the weaving of long and narrow hydroxyapatite (HAP) crystals into a unique lattice architecture composed of tightly packed parallel arrays (enamel rods). In vertebrates this highly coordinated, dynamic, biomineralization process (amelogenesis) occurs in an enamel matrix secreted by specialized cells called ameloblasts. At the early stages of amelogenesis the dominant organic component (~90%) in the enamel matrix is an ~180-residue protein called amelogenin that orchestrates the mineralization of apatite crystals via a poorly understood molecular mechanism. To address the impact of amelogenin’s structure in orchestrating biomineralization we are employing a suite of diverse, non-conventional techniques to characterize the structure of amelogenin in both the solution- and solid-state.  Thess techniques center around solution- and solid-state NMR spectroscopy and atomic force microscopy (AFM).  The ultimate results of understanding how amelogenin works in vivo is the predictive synthesis of functional materials tailored by macromolecular design.


Protein NMR spectroscopy – Solution structures and much much more

Structure solution by NMR depends on two main quantum-mechanical properties of proteins: (1) the chemical shifts of 1H, 13C, and 15N atoms are very sensitive to their chemical environment and (2) distance information obtained from the through-space dipolar interactions between protons.  The later interaction results in something called the nuclear Overhauser effect, or NOE, and the strength of this signal is inversely proportional to the 6th power of the distance between the two nuclei.  Proteins contain a lot of protons. Using of a suite of two-, three- and even four-dimensional NMR experiments, it is possible to assign most of the protons (along with the 13C and 15N atom resonances) and collect NOE values for all the protons that are generally within 6 Å of each other in space.  This NOE distance restraint and chemical shift information, along with other restraints (commonly torsion angles) are feed into a computer program (eg:  CYANA, XPLOR-NIH) to generate, through an iterative process, an ensemble of structures that satisfies all the experimental data.  The quality of these structures are assessed by online programs such as PSVS.  Data collection often requires a significant amount of high-field NMR spectrometer time (commonly 4-6 weeks) and data analysis still requires a large human component (time consuming).  While structural information can be obtained for proteins larger than 25 kDa, these efforts require more exotic isotope labeling strategies and NMR experiments. 

Solution NMR spectroscopy may be applied to solve a wide range of problems other than structure solution. Foremost is its use in studying dynamics at atomic resolution over a range of time scales.  Associated with dynamics, NMR spectroscopy is the primary technique used to discover and study intrinsically disordered proteins, a group of proteins with a wide variety of roles that may occupy ~ 25% of all protein-space.  NMR spectroscopy can be used to map protein-ligand and protein-protein interactions. Due to its sensitivity, affinity in the 100 uM to mM range, it is routinely used in high through-put screens of small molecule libraries for drug discovery.  Paramagnetic species shift or broaden the chemical shifts of near-by nuclei.  Their introduction into specific sites on a protein can be exploited in a variety of experiments to probe distances and dynamics.  Consequently, even if a crystal structure exists for a protein, a suite of NMR experiments are available to probe structure-function questions at the residue-level.


 

Professional Memberships and Activities: 
  • Associate Professor, School of Molecular Biosciences, Washington State University
  • Seattle Structural Genomics Center for Infectious Diseases
  • The Protein Society
  • International Association for Dental Research
Publications: 

2019

  • Laureanti JA, GW Buchko, S Katipamula, Q Su, JC Linehan, OA Zadvornyy, JW Peters, M O'Hagan. 2019. "Protein scaffold activates catalytic CO2 hydrogenation by a rhodium bis(diphosphine) complex." ACS Catalysis 9(1):620-625.  doi:10.1021/acscatal.8b02615
  • Tao S, Y Shin, RM Jayasinha Arachchige, GW Buchko, SD Burton, A Dohnalkova, Z Wang, WJ Shaw, BJ Tarasevich.  2019.  "Energetic basis for calcium phosphate mineralization by amelogenin variants:  insights into the origin of amelogenesis imperfecta."  Proceedings of the National Academy of Science USA (in press). 

2018

  • Buchko, GW, SVSRK Pulavarti, V Ovchinnokov, EA Shaw, SA Rettie, PJ Myler, T. Szyperski, D Baker, C Bahl.  2018.  "Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides."  Protein Science 27(9):1611-1623. doi:10.1002/pro.3453
  • Buchko GW, SN Hewitt, WC Van Voorhis, and PJ Myler. 2018. "Solution NMR Structures of Oxidized and Reduced Ehrlichia chaffeensis thioredoxin: NMR-Invisible Structure Owing to Backbone Dynamics." Acta Crystallographica. Section F 74(1):46-56. doi:10.1107/S2053230X1701799X
  • Buchko GW, RJ Arachchige, J Tao, BJ Tarasevich, and WJ Shaw. 2018. "Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rcih amelogenin peptide using an nuclear magnetic resonance spectroscopy based method."  Archives of Oral Biology 93:187-194. doi.org/10.1016/j.archoralbio.2018.06.001
  • Arachchige, RJ, SD Burton, J Lu, B Ginovask-Pangovska, L Harding, J Tao, A Dohnalkova, BJ Tarasevich, GW Buchko, WJ Shaw.  2018.  "Solid state NMR identification of intermolecular amelogenin interactions in nanospheres bound to hydroxyapatite."  Biophysical Journal 115(9):1666-1672. doi.org/10.1016/j.bpj.2018.08.027
  • Mori S, KD Green, R Choi, GW Buchko, MG Fried, S Garneau-Tsodikova. 2018. "Using MtbH-like proteins to alter substrate profile of a nonribosomal peptide adenylation enzyme."  ChemBioChem 19(20):2186-2194.  doi:10.1002/cbic.201800240

2017

  • Buchko GW, MC Clifton, E Wallace, KA Atkins, and PJ Myler. 2017. "Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus." Biomolecular NMR Assignments 11(1):51-56.  doi:10.1007/s12104-016-9719-2
  • Buchko GW, N Echols, EM Flynn, HL Ng, S Stephenson, H Kim, PJ Myler, TC Terwilliger, T Alber, and CY Kim. 2017. "Structural and biophysical characterization of the Mycobacterium tuberculosis protein Rv0577, a protein associated with neutral red staining of virulent tuberculosis strains and homologue of the Streptomyces coelicolor protein KbpA." Biochemistry 56(30):4015-4027.  doi:10.1021/acs.biochem.7b00511
  • Boralugodage N, RM Jayasinha Arachchige, A Dutta, GW Buchko, and WJ Shaw. 2017. "Evaluating the Role of Acidic, Basic, and Polar Amino Acids and Dipeptides on a Molecular Electrocatalyst for H2 Oxidation." Catalysis Science & Technology 7(5):1108-1121.  doi:10.1039/c6cy02579j
  • Zerfass C, GW Buchko, WJ Shaw, S Hobe, and H Paulsen. 2017. "Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P5S3 during silicic acid condensation and silica decondensation." Proteins. Structure, Function, and Bioinformatics 85(11):2111-2126.  doi:10.1002/prot.25366

2016

  • Buchko GW, A Perkins, D Parsonage, LB Poole, and PA Karplus. 2016. "Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics." Biomolecular NMR Assignments 10(1):57-61.  doi:10.1007/s12104-015-9637-8
  • Reback ML, B Ginovska-Pangovska, GW Buchko, A Dutta, N Priyadarshani, BL Kier, ML Helm, S Raugei, and WJ Shaw. 2016. "Investigating the role of chain and linker length on the catalytic activity of an H2 production catalyst containing a b-hairpin peptide." Journal of Coordination Chemistry 69(11-13):1730-1747.  doi:10.1080/00958972.2016.1188924
  • Bhardwaj G, VK Mulligan, CD Bahl, JM Gilmore, P Harvey, O Cheneval, GW Buchko, SV Pulavarti, Q Kass, A Eletsky, PS Huang, WA Johnsen, P Griesen, GJ Rocklin, Y Song, TW Linsky, A Watkins, SA Rettie, X Xu, LP Carter, RA Bonneau, JM Olsen, E Coutsias, CE Correnti, T Szyperski, DJ Craik, and D Baker. 2016. "Accurate de novo design of hyperstable constrained peptides." Nature 538(7625):329-335.  doi:10.1038/nature19791
  • Priyadarshani N, A Dutta, B Ginovska-Pangovska, GW Buchko, MJ O'Hagan, S Raugei, and WJ Shaw. 2016. "Achieving Reversible H2/H+ Interconversion at Room Temperature with Enzyme-Inspired Molecular Complexes: A Mechanistic Study." ACS Catalysis 6(9):6037-6049. doi:10.1021/acscatal.6b01433

2015

  • Buchko GW, A Yee, A Semesi, PJ Myler, CH Arrowsmith, and R Hui. 2015. "Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum." Acta Crystallographica. Section F F71(5):514-521.  doi: 10.1107/S2053230X1402799X
  • Buchko GW, and WJ Shaw. 2015. "Improved protocol to purify untagged amelogenin - Application to murine amelogenin containing the equivalent P70 ? T point mutation observed in human amelogenesis imperfecta." Protein Expression and Purification 105(1):14-22. doi:10.1016/j.pep.2014.09.020
  • Buchko GW, TE Edwards, SN Hewitt, I Phan, WC Van Voorhis, SI Miller, and PJ Myler. 2015. "Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS - "missing" resonances at the dimer interface." Biomolecular NMR Assignments 9(2):381-385.  doi:10.1007/s12104-015-9614-2 
  • Buchko GW, J Abendroth, MC Clifton, H Robinson, Y Zhang, SN Hewitt, BL Staker, TE Edwards, WC Van Voorhis, and PJ Myler. 2015. "Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum, the protozoal parasite responsible for cryptosporidiosis." Acta Crystallographica. Section F F71(5):522-530. doi:10.1107/S2053230X14028210
  • Tao J, GW Buchko, WJ Shaw, J De Yoreo, and BJ Tarasevich. 2015. "Sequence-defined Energetic Shifts Control the Disassembly Kinetics and Microstructure of Amelogenin Adsorbed onto Hydroxyapatite (100)." Langmuir 31(38):10451-10460. doi:10.1021/acs.langmuir.5b02549
  • Baugh L, I Phan, DW Begley, MC Clifton, B Armour, DM Dranow, BM Taylor, MM Muruthi, J Abendroth, JW Fairman, D Fox III, SH Dieterich, BL Staker, AS Gardberg, R Choi, SN Hewitt, AJ Napuli, J Myers, L Barrett, Y Zhang, M Ferrell, E Mundt, K Thompkins, N Tran, S Lyons-Abbott, A Abramov, A Sekar, D Serbzhinskiy, D Lorimer, GW Buchko, R Stacy, LJ Stewart, TE Edwards, WC Van Voorhis, and PJ Myler. 2015. "Increasing the Structural Coverage of Tuberculosis Drug Targets." Tuberculosis 95(2):142-148.  doi:10.1016/j.tube.2014.12.003
  • Staker BL, GW Buchko, and PJ Myler. 2015. "Recent contributions of structure-based drug design to the development of antibacterial compounds." Current Opinion in Microbiology 27(1):133-138.  doi:10.1016/j.mib.2015.09.003
  • Tarasevich BJ, JS Philo, NK Maluf, S Krueger, GW Buchko, G Lin, and WJ Shaw. 2015. "The Leucine-Rich Amelogenin Protein (LRAP) is primarily monomeric and unstructured in physiological solution." Journal of Structural Biology 190(1):81-91. doi:10.1016/j.jsb.2014.10.007

2014

  • Lu J, SD Burton, Y Xu, GW Buchko, and WJ Shaw. 2014. "The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength." Frontiers in Physiology 5:254. doi:10.3389/fphys.2014.00254 
  • Zhang Y, Y Zheng, L Qin, S Wang, GW Buchko, and MR Garavito. 2014. "Structural characterization of a ß-hydroxyacid dehydrogenase from Geobacter sulfurreducens and Geobacter metallireducens with succinic semialdehyde reductase activity." Biochimie 104:61-69.  doi:10.1016/j.biochi.2014.05.002 
  • Reback ML, GW Buchko, BL Kier, B Ginovska-Pangovska, Y Xiong, S Lense, J Hou, JA Roberts, CM Sorensen, S Raugei, TC Squier, and WJ Shaw. 2014. "Enzyme Design From the Bottom Up: An Active Nickel Electrocatalyst with a Structured Peptide Outer Coordination Sphere." Chemistry - A European Journal 20(6):1510-1514.  doi:10.1002/chem.201303976

2013

  • Buchko GW, G Lin, BJ Tarasevich, and WJ Shaw. 2013. "A solution NMR investigation into the impaired self-assembly properties of two murine amelogenins containing the point mutations T21?I or P41?T." Archives of Biochemistry and Biophysics 537(2):217-224. doi:10.1016/j.abb.2013.07.015
  • Buchko GW, SN Hewitt, WC Van Voorhis, and PJ Myler. 2013. "Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia." Journal of Biomolecular NMR 57(4):369-374.  doi:10.1007/s10858-013-9797-8
  • Buchko GW, A Jain, ML Reback, and WJ Shaw. 2013. "Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-NH2 in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol." Canadian Journal of Chemistry 91(6):406-413.  doi:10.1139/cjc-2012-0429
  • Buchko GW, J Abendroth, H Robinson, Y Zhang, SN Hewitt, TE Edwards, WC Van Voorhis, and PJ Myler. 2013. "Crystal structure of a macrophage migration inhibitory factor from Giardia lamblia." Journal of Structural and Functional Genomics 14(2):47-57. doi:10.1007/s10969-013-9155-9
  • Lu J, Y Xu, GW Buchko, and WJ Shaw. 2013. "Mineral Association Changes the Secondary Structure and Dynamics of Murine Amelogenin." Journal of Dental Research 92(11):1000-1004.  doi:10.1177/0022034513504929 
  • Baugh L, LA Gallagher, R Patrapuvich, MC Clifton, AS Gardberg, TE Edwards, B Armour, DW Begley, SH Dieterich, DM Dranow, J Abendroth, JW Fairman, D Fox III, BL Staker, I Phan, A Gillespie, R Choi, S Nakazawa-Hewitt, MT Nguyen, AJ Napuli, L Barrett, GW Buchko, R Stacy, PJ Myler, LJ Stewart, C Manoil, and WC Van Voorhis. 2013. "Combining Functional and Structural Genomics to Sample the Essential Burkholderia Structome." PLoS One 8(1):e53851.  doi:10.1371/journal.pone.0053851
  • Sagaram US, K El-Mounadi, GW Buchko, HR Berg, J Kaur, R Pandurangi, TJ Smith, and D Shah. 2013. "Structural and functional studies of a phosphatidic acid-binding antifungal plant defensin MtDef4: Identification of an RGFRRR motif governing fungal cell entry." PLoS One 8(12):e82485.  doi:10.1371/journal.pone.0082485
  • Zhang Y, A Gardberg, TE Edwards, B Sankaran, H Robinson, SM Varnum, and GW Buchko. 2013. "Structural Insights into the Functional Role of the Hcn Sub-domain of the Receptor-Binding Domain of the Botulinum Neurotoxin Mosaic Serotype C/D." Biochimie 95(7):1379-1385.  doi:10.1016/j.biochi.2013.03.006

2012

  • Buchko GW, and H Robinson. 2012. "Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family." FEBS Letters 586(4):350-355. doi:10.1016/j.febslet.2012.01.037 
  • Buchko GW, H Kim, PJ Myler, TC Terwilliger, and CY Kim. 2012. "Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis ." Biomolecular NMR Assignments 6(1):43-46.  doi:10.1007/s12104-011-9322-5
  • Buchko GW, I Phan, L Cron, R Stacy, LJ Stewart, BL Staker, TE Edwards, G Varani, WC Van Voorhis, and PJ Myler. 2012. "Behind Every Good Metabolite there is a Great Enzyme (and perhaps a structure)." Metabolomics 2(6):Article No. e124. 
  • Jain A, GW Buchko, ML Reback, MJ O'Hagan, B Ginovska-Pangovska, JC Linehan, and WJ Shaw. 2012. "Active Hydrogenation Catalyst with a Structured, Peptide-Based Outer-Coordination Sphere." ACS Catalysis 2(10):2114-2118.  doi:10.1021/cs3004177
  • Jin H, Y Zhang, GW Buchko, SM Varnum, H Robinson, TC Squier, and PE Long. 2012. "Structure Determination and Functional Analysis of a Chromate Reductase from Gluconacetobacter hansenii." PLoS One 7(8):Article No. e42432. doi:10.1371/journal.pone.0042432

2011

  • Buchko GW, I Phan, PJ Myler, TC Terwilliger, and CY Kim. 2011. "Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c." Archives of Biochemistry and Biophysics 506(2):150-156.  doi:10.1016/j.abb.2010.12.001
  • Buchko GW, SN Hewitt, AJ Napuli, WC Van Voorhis, and PJ Myler. 2011. "Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis." Acta Crystallographica. Section F 67(9):1129-1136. doi:10.1107/S1744309111006336
  • Buchko GW, SN Hewitt, AJ Napuli, WC Van Voorhis, and PJ Myler. 2011. "Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis." Acta Crystallographica. Section F 67(9):1148-1153. doi:10.1107/S1744309111008189
  • Buchko GW, TE Edwards, J Abendroth, TL Arakaki, L Law, AJ Napuli, SN Hewitt, WC Van Voorhis, LJ Stewart, BL Staker, and PJ Myler. 2011. "Structure of a Nudix hydrolase (MutT) in the Mg2+ -bound state from Bartonella henselae, the bacterium responsible for cat scratch fever." Acta Crystallographica. Section F 67(9):1078-1083.  doi:10.1107/S1744309111011559 
  • Buchko GW. 2011. "Structural genomics - A goldmine of blueprints for structure-based drug design." Metabolomics 1(2):104e.  doi:10.4172/2153-0769.1000104e
  • Zhang Y, GW Buchko, L Qin, H Robinson, and SM Varnum. 2011. "Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions." Biochemical and Biophysical Research Communications 404(1):407-412.  doi:10.1016/j.bbrc.2010.11.134
  • Stacy R, DW Begley, I Phan, BL Staker, WC Van Voorhis, G Varani, GW Buchko, LJ Stewart, and PJ Myler. 2011. "Structural genomics of infectious disease drug targets: the SSGCID." Acta Crystallographica. Section F 67(9):979-984.  doi:10.1107/S1744309111029204 

2010

  • Buchko GW, CY Kim, TC Terwilliger, and PJ Myler. 2010. "Solution Structure of Rv2377c-Founding Member of the MbtH-Like Protein Family." Tuberculosis 90(4):245-251. 
  • Buchko GW, H Robinson, J Abendroth, BL Staker, and PJ Myler. 2010. "Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): Profound asymmetry in the crystal structure of the ‘open’ state ." Biochemical and Biophysical Research Communications 394(4):1012-1017. 
  • Buchko GW. 2010. "Circular Dichrosim Studies on the Deinococcus Radiodurans Nudix Hydrolase DR_0079: an Atypical Thermal Melt." Protein and Peptide Letters 17(7):831-835. 
  • Buchko GW, BJ Tarasevich, J Roberts, ML Snead, and WJ Shaw. 2010. "A Solution NMR Investigation into the Murine Amelogenin Splice-Variant LRAP (Leucine-Rich Amelogenin Protein)." Biochimica et Biophysica Acta--Proteins and Proteomics 1804(9):1768-1774. 
  • Buchko GW, G Niemann, ES Baker, ME Belov, RD Smith, F Heffron, JN Adkins, and JE McDermott. 2010. "A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins." Molecular Biosystems 6(12):2448-2458.  doi:10.1039/c0mb00097c
  • Tang Z, H Wu, JR Cort, GW Buchko, Y Zhang, Y Shao, IA Aksay, J Liu, and Y Lin. 2010. "Constraint of DNA on Functionalized Graphene Improves Its Biostability and Specificity." Small 6(11):1205-1209.  doi:10.1002/smll.201000024
  • Zhang Y, GW Buchko, L Qin, H Robinson, and SM Varnum. 2010. "Structural analysis of the receptor binding domain of botulinum neurotoxin serotype D." Biochemical and Biophysical Research Communications 401:498-503.  doi:10.1016/j.bbrc.2010.09.063
  • Zhang Y, X Gao, L Qin, GW Buchko, H Robinson, and SM Varnum. 2010. "High-level expression, purification, crystallization and preliminary X-ray crystallographic studies of the receptor binding domain of botulinum neurotoxin serotype D." Acta Crystallographica. Section F 66(12):1610-1613.  doi:10.1107/S1744309110039874

2009

  • Buchko GW, H Robinson, and A Addlagatta. 2009. "Structural characterization of the protein cce_0567 from Cyanothece 51142, a metalloprotein associated with nitrogen fixation in the DUF683 family." Biochimica et Biophysica Acta--Proteins and Proteomics 1794(4):627-633. 
  • Buchko GW, SN Hewitt, AJ Napuli, WC Van Voorhis, and PJ Myler. 2009. "Backbone and side chain 1H, 13C, and 15N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei. ." Biomolecular NMR Assignments 3(2):163-166. doi:10.1007/s12104-009-9165-5
  • Buchko GW. 2009. "Pentapeptide Repeat Proteins and Cyanobacteria." In Handbook on Cyanobacteria: Biochemistry, Biotechnology and Applications, pp. 233-257.  Nova Science Publishers, Hauppauge, NY. 
  • Harvey SD, GW Buchko, RB Lucke, CW Wright, AM Melville, AJ Scott, and BW Wright. 2009. "The Structure and Purity of a Reference Dye Standard used for Quantification of C.I. Solvent Red 164 in Fuels." Dyes and Pigments 82(3):307-315. doi:10.1016/j.dyepig.2009.01.015
  • Myler PJ, R Stacy, LJ Stewart, BL Staker, WC Van Voorhis, G Varani, and GW Buchko. 2009. "The Seattle Structure Genomics Center for Infectious Disease (SSGCID)." Infectious Disorders Drug Targets 9(5):493-506. 
  • Webb-Robertson BJM, LA McCue, N Beagley, JE McDermott, DS Wunschel, SM Varnum, JZ Hu, NG Isern, GW Buchko, K Mcateer, JG Pounds, SJ Skerret, D Liggitt, and CW Frevert. 2009. "A Bayesian Integration Model of High-Throughput Proteomics and Metabolomics Data for Improved Early Detection of Microbial Infections." In Pacific Symposium on Biocomputing, vol. 14, pp. 451-463.  World Scientific Publishing Co., Singapore, Singapore. 

2008

  • Buchko GW, H Robinson, HB Pakrasi, and MA Kennedy. 2008. "Insights into the structural variation between pentapeptide repeat proteins - Crystal structure of Rfr23 from Cyanothece 51142." Journal of Structural Biology 162(1):184-192. 
  • Buchko GW, O Litvinova, H Robinson, AF Yakunin, and MA Kennedy. 2008. "Functional and structural characterization of DR_0079 from Deinococcus radiodurans, a novel Nudix hydrolase with a preference for cytosine (deoxy) ribonucleoside 5'-di- and triphosphates." Biochemistry 47(25):6571-82. 
  • Buchko GW, JG Bekhazi, JR Cort, NB Valentine, ML Snead, and WJ Shaw. 2008. "1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein. ." Biomolecular NMR Assignments 2(1):89-91. 
  • Buchko GW, and HJ Sofia. 2008. "Backbone 1H, 13C, and 15N NMR assignments for the Cyanothece 51142 protein cce_0567: a protein associated with nitrogen fixation in the DUF683 family." Biomolecular NMR Assignments 2:25-28. 
  • Buchko GW, BJ Tarasevich, JG Bekhazi, ML Snead, and WJ Shaw. 2008. "A Solution NMR Investigation into the Early Events of Amelogenin Nanosphere Self-Assembly Initiated with Sodium Chloride or Calcium Chloride." Biochemistry 47(50):13215-13222. doi:10.1021/bi8018288
  • Buchko GW. 2009. "Pentapeptide repeat proteins and cyanobacteria" In:  Gault PM and Marler HJ (eds.) Handbook on Cyanobacteria:  Biochemistry, Biotechnology and Applications.  Nova Science Publishers, Inc., New York NY, pp 233-257.

2007

  • Buchko GW, S Ni, NM Lourette, RC Reeves, and MA Kennedy. 2007. "NMR resonance assignments of the human high mobility group protein HMGA1." Journal of Biomolecular NMR 38(2):185.  doi:10.1007/s10858-006-9116-8

2006

  • Buchko GW, and J Cadet. 2006. "Identification of the a and ß Anomers of 1-(2-Deoxy-D-Erythro-Pentofuranosyl)-Oxaluric Acid at the Site of Riboflavin-mediated Photooxidation of Guanine in 2'-Deoxyguanosine and Thymidylyl-(3'-5')-2'-Deoxyguanosine." Photochemistry and Photobiology 82(1):191-199. 
  • Buchko GW, CY Kim, TC Terwilliger, and MA Kennedy. 2006. "Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis. ." Journal of Bacteriology 188(16):5993-6001.  doi:10.1128/JB.00460-06
  • Buchko GW, H Robinson, S Ni, HB Pakrasi, and MA Kennedy. 2006. "Cloning, expression, crystallization and preliminary crystallographic analysis of a pentapeptide-repeat protein (Rfr23) from bacterium Cyanothece 511421." Acta Crystallographica. Section F 62(12):1251-1254.  doi:10.1107/S174430910604663X
  • Buchko GW, S Ni, H Robinson, EA Welsh, HB Pakrasi, and MA Kennedy. 2006. "Characterization of two potentially universal turn motifs that shape the repeated five-residues fold - Crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142." Protein Science 15(11):2579-2595. 

2005

  • Buchko GW, K McAteer, SS Wallace, and MA Kennedy. 2005. "Solution-state NMR Investigation of DNA Binding Interactions in Escherichia coli Formamidopyrimidine-DNA Glycosylase (Fpg): A Dynamic Description of the DNA/Protein Interface ." DNA Repair 4(3):327-339. 

2004

  • Buchko GW, S Ni, SR Holbrook, and MA Kennedy. 2004. "Solution Structure of Hypothetical Nudix Hydrolase DR0079 from Extremely Radiation-Resistant Deinococcus radiodurans Bacterium." Proteins. Structure, Function, and Bioinformatics 56(1):28-39. 
  • McAteer K, A Aceves Gaona, R Michalczyk, GW Buchko, NG Isern, LA Silks, JH Miller, and MA Kennedy. 2004. "Compensating Bends in a 16 base-pair DNA Oligomer Containing a T3A3 Segment: A NMR Study of Global DNA Curvature." Biopolymers 75(6):497-511. 

2003

  • Buchko GW, S Ni, SR Holbrook, and MA Kennedy. 2003. "H-1, C-13, and N-15 NMR assignments of the hypothetical Nudix protein DR0079 from the extremely radiation-resistant bacterium Deinococcus radiodurans." Journal of Biomolecular NMR 25(2):169-170. 
  • Daughdrill GW, GW Buchko, MV Botuyan, CH Arrowsmith, MS Wold, MA Kennedy, and DF Lowry. 2003. "Chemical shift changes provide evidence for overlapping single-stranded DNA and XPA binding sites on the 70 kDa subunit of human replication protein A." Nucleic Acids Research 31(14):4176-4183. 
  • Holbrook EL, U Schulze-Gahmen, GW Buchko, S Ni, MA Kennedy, and SR Holbrook. 2003. "Purification, crystallization and preliminary X-ray analysis of two Nudix hydrolases from Deinococcus radiodurans." Acta Crystallographica. Section D, Biological Crystallography 59(Pt.4):737-740. 

2002

  • Buchko GW, and M Weinfeld. 2002. "DNA-Targeted 2-Nitroimidazoles: Studies of the Influence of the Phenanthridine-Linked Nitroimidazoles, 2-NLP-3 and 2-NLP-4, on DNA Damage Induced by Ionizing Radiation." Radiation Research 158 (3):302-310. 
  • Buchko GW, SS Wallace, and MA Kennedy. 2002. "Base excision repair: NMR backbone assignments of Escherichia coli formamidopyrimidine-DNA glycosylase." Journal of Biomolecular NMR 22(3):301-302. 

2001

  • Buchko GW, and MA Kennedy. 2001. "Hydroxyapatite Elution Behavior of Human Nucleotide Excision Repair Protein XPA and Fragments of XPA." Protein and Peptide Letters 8 (5)(2001):357-365. 
  • Buchko GW, CS Tung, K Mcateer, NG Isern, LD Spicer, and MA Kennedy. 2001. "DNA-XPA Interactions: A 31P NMR Study of dCCAATAACC Association With the Minimal DNA-Binding Domain (M98-F219) of the Nucleotide Excision Repair Protein XPA." Nucleic Acids Research 29(12):2635-2643. 
  • Buchko GW, NG Isern, LD Spicer, and MA Kennedy. 2001. "Human Nucleotide Excision Repair Protein XPA: NMR Spectroscopic Studies of an XPA Fragment Containing the ERCC1-Binding Region and the Minimal DNA-Binding Domain (M59-F219)." Mutation Research 486(1):1-10. 
  • Lipton AS, GW Buchko, JA Sears, Jr, MA Kennedy, and PD Ellis. 2001. "Zn-67 Solid-State NMR Spectroscopy of the Minimal DNA Binding Domain of Human Nucleotide Excision Repair Protein XPA." Journal of the American Chemical Society 123(5):992-993. 

2000

  • Buchko GW, A Rozek, P Kanda, MA Kennedy, and RJ Cushley. 2000. "Structural Studies of a Baboon (Papio sp.) Plasma Protein Inhibitor of Cholesteryl Ester Transferase." Protein Science 9:1548-1558. 
  • Buchko GW, NJ Hess, and MA Kennedy. 2000. "Cadmium Mutagenicity and Human Nucleotide Excision Repair Protein XPA: CD, EXAFS, and 1H/15N NMR Spectroscopic Studies on the Zinc (II) and Cadmium (II) Associated Minimal DNA-Binding Domain." Carcinogenesis 21(5):1051-1057. 
  • Buchko GW, NJ Hess, and MA Kennedy. 2000. "Human Nucleotide Excision Repair Protein XPA: Summary of EXAFS Studies On the Zn (II), Co (II), and Cd (II) Associated Minimal DNA-Binding Domain." Protein and Peptide Letters 7(1):49-56. 
  • Buchko GW, NJ Hess, V Bandaru, SS Wallace, and MA Kennedy. 2000. "Spectroscopic Studies of Zinc (II) and Cobalt (II) Associated Escherichia Coli Formamidopyrimidine-DNA Glycosylase: Extended X-Ray Absorption Fine Structure Evidence for a Metal-Binding Domain." Biochemistry 39:12441-12449. 

1999

  • Buchko GW, GW Daughdrill, R De Lorimier, S Rao B K, NG Isern, JM Lingbeck, JS Taylor, MS Wold, M Gochin, LD Spicer, DF Lowry, and MA Kennedy. 1999. "Interactions of Human Nucleotide Excision Repair Protein XPA with DNA and RPA70 Delta c327: Chemical Shift Mapping and N-15 NMR Relaxation Studies." Biochemistry 38(46):15116-15128. 
  • Buchko GW, LM Iakoucheva, MA Kennedy, EJ Ackerman, and NJ Hess. 1999. "Extended X-ray Absorption Fine Structure Evidence for a Single Metal Binding Domain in Xenopus Laevis Nucleotide Excision Repair Protein XPA." Biochemical and Biophysical Research Communications 254(1):109-113. 

1998

  • Buchko GW, S Ni, BD Thrall, and MA Kennedy. 1998. "Structural Features of the Minimal DNA Binding Domain (M98-F219) of Human Nucleotide Excision Repair Protein XPA." Nucleic Acids Research 26(11):2779-2788. 
  • Buchko GW, A Rozek, DW Hoyt, RJ Cushley, and MA Kennedy.  1998. "The use of sodium dodecl sulfate to model the apolipoprotein environment.  Evidence for pleptide-SDS complexes using pulsed-field-gradient NMR spectroscopy.  Biochemica Biophysica Acta 1392:101-108.
  • Hess NJ, GW Buchko, SD Conradson, FJ Espinosa, S Ni, BD Thrall, and MA Kennedy.  1998. "Human nucleotide excision repair protein XPA:  Extended X-ray absorption fine structure evidence for a metal-binding domain.  Protein Science 7:1970-1975.
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