Tom Terwilliger, Selected Publications

 

Publications:

Can I solve my structure by SAD phasing? Anomalous signal in SAD phasing. Terwilliger, T. C., Bunkóczi, G., Hung, L.-W., Zwart, P. H., Smith, J. L., Akey, D. L., Adams, P.D. 2016. Acta Cryst. D72, 346-358.
 
Outcome of the First wwPDB/CCDC/D3R Ligand Validation Workshop.  Adams, P.D., et al. 2016. Structure 24, 502-408.
 
A suite of engineered GFP molecules for oligomeric scaffolding. Leibly, D. J., Arbing, M. A., Pashkov, I., DeVore, N., Waldo, G.S., Terwilliger, T.C., Yeates, T.O. 2015. Structure 23, 1754-1768.
 
X-ray structure determination using low-resolution electron microscopy maps for molecular replacement. Jackson, R. N., Terwilliger, T. C., Read, R. J., Wiedenheft, B. 2015. Nature Protocols 10, 1275-1284.
 
Macromolecular X-ray structure determination using weak single-wavelength anomalous data. Bunkóczi, G., McCoy, A.J., Echols, N., Grosse-Kunstleve, R.W., Adams, P.D., Holton, J. M., Read, R.J., Terwilliger, T.C. 2015. Nature Methods 12, 127-130.
 
Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis.  Prigozhin, D.M., Krieger, I.V., Huizar, J.P., Mavrici, D., Waldo, G.S., Hung, L.W., Sacchettini, J.C., Terwilliger, T.C., Alber, T. 2014. PLos ONE 9, e116249.
 
Crystal structure of the CRISPR RNA-guided surveillance complex from Escherichia coli. Jackson, R.N., Golden, S.M., van Erp, P.B.G., Carger, J., Westra, E.R., Brouns, S.J.J., van der Oost, J., Terwilliger, T.C., Read, R.J., Widenheft, B. 2014. Science 345, 1473-1479.
 
 
Crystal structure of AcrB complexed with linezolid at 3.5 Å resolution. Hung, L.-W., Kim, H.-B., Murakami, S., Gupta, G., Kim, C.-Y., Terwilliger, T.C. 2013. J. Struct. Func. Genomics 14, 71-75.
 
Improved Crystallographic Structures Using Extensive Combinatorial Refinement. Nwachukwu, J. C., Southern, M. R., Kiefer, J. R., Afonine, P. V., Adams, P. D., Terwilliger, T. C., Nettles, K. W. 2013. Structure, 21, 1923-1930.
 
Improved low-resolution crystallographic refinement with Phenix and RosettaDiMaio, F., Echols, N., Headd, J. J., Terwilliger, T. C., Adams, P. D., & Baker, D. (2013).  Nature Methods 10, 1102-1104.
 
Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabTEdayathumangalam, R., Wu, R., Garcia, R., Wang, Y., Wang, W., Kreinbring, C. A., Bach, A., Liao, J., Stone, T., Terwilliger, T.C., Hoang, Q.Q., Belitsky, B.R., Petsko, G.A., Liu, D. (2013).  Proceedings of the National Academy of Sciences, 110, 17820-17825.
 
Improving molecular replacement by density and energy guided protein structure optimization  DiMaio, F., Terwilliger, T.C., Read, R.J., Wlodawer, A., Oberdorfer, G., Wagner, U., Valkov, E., Alon, A., Fass, D., Axelrod, H.L., Das, D., Vorobiev, S.M., Iwai, H., Pokkuluri, P.R., D. Baker (2011). Nature 473, 540-543.
 
PHENIX: a comprehensive Python-based system for macromolecular structure solution. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., Zwart, P. H. 2010. Acta Cryst. D66, 213-221. 
 
New Molecular Reporters for Rapid Protein Folding Assays. Cabantous S, Rogers Y, Terwilliger T, Waldo GS (2008). PLoS ONE 3(6): 1-10 (e2387).
 
Protein production and purification. Structural Genomics Consortium et al.,. Nature Methods. 2008, 135-46.
 
Functional linkages can reveal protein complexes for structure determination. Kim, S.M., Bowers, P.M., Pal, .D, Strong, M., Terwilliger, T.C., Kaufmann, M., Eisenberg, .D. (2007).  Structure 15, 1079-1089.
 
Is one solution good enoughFurnham, N., Blundell, T. L., DePristo, M. A., Terwilliger, T.C. (2006). Nature Structural & Molecular Biology 13, 184 – 185.
 
Engineering and characterization of a superfolder green fluorescent proteinPédelacq, J.-D., Cabantous, S., Tran, T., Terwilliger, T.C., Waldo, G. S. (2006). Nature Biotechnology, 24, 79-88.
 
Structure of pyrR (Rv1379) from Mycobacterium tuberculosis: a persistence gene and protein drug target. Kantardjieff KA, Vasquez C, Castro P, Warfel NM, Rho BS, Lekin T, Kim CY, Segelke BW, Terwilliger TC, Rupp B. 2005. Acta Cryst D 61, 355-364.
 
Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Cabantous, S., Terwilliger, T. C., Waldo, G. S. (2005). Nature Biotechnology 23, 102-107.
 
Structures and technology for biologists.Terwilliger, T. C. 2004. Nature Structural and Molecular Biology 11, 296-297.
 
The Crystal Structure of the First Enzyme in the Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase, from M. tuberculosis. Chaudhuri, B. N., Sawaya, M. R., Kim, C.-Y., Waldo, G. S., Park, M. S., Terwilliger, T. C. & Todd O. Yeates, T. O. 2003. Structure, 11, 753-764
 
Engineering soluble proteins for structural genomicsPédelacq, J.-D., Piltch, E., Liong, E. E., Berendzen, J., Kim, C.-Y., Rho, B.-S., Park, M. S., Terwilliger, T. C. & Waldo, G. S (2012).  Nature Biotechnology, 20, 927-932.
 
Structural Genomics in North AmericaTerwilliger, T. C. (2000). Nature Structural Biology 7, 935-939.
 
Maximum-likelihood density modificationTerwilliger, T. C.  (2000). Acta Crystallographica, D55, 965-972.​
 
Automated MAD and MIR structure solutionTerwilliger, T. C. and Berendzen, J.  (1999). Acta Crystallographica, D55, 849-861.
 
Rapid protein-folding assay using green fluorescent proteinWaldo, G., Standish, B. M., Berendzen, J. & Terwilliger, T. C. (1999)  Nature Biotechnology 17, 691-695.
 
Structure Of Translation Initiation-Factor 5a From Pyrobaculum-Aerophilum At 1.75 Angstrom Resolution. Peat T.S., Newman J, Waldo G.S, Berendzen J., Terwilliger T.C.  (1998) Structure 6, 1207-1214.
 
Potential use of additivity of mutational effects in simplifying protein engineering. Skinner, M. M. and Terwilliger, T. C.  (1996)  Proc. Natl. Acad. Sci. USA 93, 10753-10757.
 
Structure of the gene V protein of bacteriophage f1 determined by multiwavelength X- ray diffraction on the selenomethionyl protein.  Skinner, M. M., Zhang, H., Leschnitzer, D. H. , Guan, Y., Bellamy, H., Sweet, R. M., Gray, C. W., Konings, R. N. H., Wang, A. H.-J., and T. C. Terwilliger  (1994).  Proc. Natl. Acad. Sci. USA 91, 2071-2075. 
 
Engineering multiple properties of a protein by combinatorial mutagenesis. Sandberg, W. S and T. C. Terwilliger  (1993). Proc. Natl. Acad. Sci. USA 90, 8367-8371.
 
Energetics of repacking a protein interior.  Sandberg, W. S. and T. C. Terwilliger  (1991).  Proc. Natl. Acad. Sci. USA 88, 1706-1710.
 
Influence of interior packing and hydrophobicity on the stability of a protein.  Sandberg, W. S. and  T. C. Terwilliger  (1989). Science 245, 54-57.
 
Surface structure recognized for covalent modification of the aspartate receptor in chemotaxis.  Terwilliger, T. C., Wang, J. Y. and D. E. Koshland, Jr.  (1986).  Proc. Natl. Acad. Sci.  USA 83, 6707-6710.
 
The hydrophobic moment detects  periodicity in protein hydrophobicity. Eisenberg, D., Weiss, R. M., and T. C.  Terwilliger.  (1984).  Proc. Natl. Acad. Sci. USA 81, 140-144.
 
The helical hydrophobic moment: a measure of the amphiphilicity of a helix.  Eisenberg, D., Weiss, R. M., and T. C. Terwilliger  (1982).  Nature 299, 371-374.​
 

Back to Research Team Page

Back to Human Health and Agriculture Research Page

© 2017 New Mexico Consortium