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terwilliger at lanl dot gov

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(505) 665-4650

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Thomas C. Terwilliger

Structural Biology

Tom Terwilliger graduated magna cum laude in Physics from Harvard College in 1978. He obtained his PhD on the structure of melittin from bee venom with David Eisenberg at UCLA in 1981. He was a Helen Hay Whitney Postdoctoral Fellow with Daniel E. Koshland, Jr., at UC Berkeley from 1981-1985, then a Presidential Young Investigator at the University of Chicago from 1985-1990, and has been on the staff of Los Alamos National Laboratory since 1991. He is now a Laboratory Fellow and works on Structural Genomics and methods for X-ray crystallography.

Research Interests

  • Structural genomics: Proteins are the molecular machines of life, and a knowledge of their three-dimensional structures is crucial for understanding how they work. >>> read more...
  • TB Structural Genomics Consortium:The TB Structural Genomics Consortium is a worldwide consortium of hundreds of scientists from around the world devoted to determining structures of proteins from the pathogenic organism M. tuberculosis. Our group founded and led the TB SGC for its first 5 years as part of phase 1 of the NIH Protein Structure Initiative. >>> read more...
  • The Integrated Center for Structure and Function Innovation: Our Los Alamos group leads the ISFI, a consortium of scientists developing methods for determining protein structures reliably and rapidly. >>>read more...
  • Methods development for macromolecular crystallography: Our group and our colleagues have developed algorithms and software for analyzing X-ray diffraction data from macromolecules such as proteins and nucleic acids and determining their 3-dimensional structures. >>> read more...

Representative Publications

Anderson, D., Terwilliger, T. C., Wickner, W. and D. Eisenberg.  (1980).  Melittin forms crystals which are suitable for high-resolution x-ray structural analysis and which reveal a molecular 2-fold axis of symmetry.  J. Biol Chem.  255, 2578-2582.

Terwilliger, T. C. and S. Clarke.  (1981).  Methylation of membrane proteins in human erythrocytes: Identification and characterization of polypeptides methylated in lysed cells.  J. Biol. Chem.  256, 3067-3076.

Terwilliger, T. C. and A. K. Solomon.  (1981).  Osmotic water permeability of human red cells.  J. General Physiol.  77, 549-570.

Eisenberg, D., Weiss, R. M., Terwilliger, T. C. and W. Wilcox.  (1982).  Hydrophobic moments and protein structure.  Faraday Symp. Chem. Soc. 17, 109-120.

Eisenberg, D., Weiss, R. M., and T. C. Terwilliger  (1982).  The helical hydrophobic moment: a measure of the amphiphilicity of a helix.  Nature 299, 371-374.  (537 citations).

Terwilliger, T. C., Weissman, L, and D. Eisenberg.  (1982).  The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities.  Biophys. J.  37, 353-361.  (288 citations).

Terwilliger, T. C. and D. Eisenberg.  (1982).  The structure of melittin.  I. Structure determination and partial refinement.  J. Biol. Chem.  257, 6010-6015.  (178 citations).

Terwilliger, T. C. and D. Eisenberg.  (1982).  The structure of melittin. II.  Interpretation of the structure.  J. Biol. Chem.  257, 6016-6022.  (304 citations).

Terwilliger, T. C., Bogonez, E., Wang, E. A., and D. E. Koshland, Jr.  (1983).  Sites of methyl esterification on the aspartate receptor involved in bacterial chemotaxis.  J. Biol. Chem.  258, 9608-9611.

Terwilliger, T. C. and D. Eisenberg.  (1983).  Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions.  Acta Crystallographica A39, 813-817.  (194 citations).

Terwilliger, T. C. and D. E. Koshland, Jr.  (1984).  Sites of methyl esterification and deamination on the aspartate receptor involved in chemotaxis.  J. Biol. Chem. 259, 7719-7725.

Eisenberg, D., Weiss, R. M., and T. C.  Terwilliger.  (1984).  The hydrophobic moment detects  periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA 81, 140-144.  (566 citations).

Terwilliger, T. C., Wang, J. Y. and D. E. Koshland, Jr.  (1986).  Kinetics of receptor modification: the multiply methylated aspartate receptors involved in bacterial chemotaxis.  J. Biol. Chem. 261, 10814-10820.

Terwilliger, T. C., Bollag, G. E., Sternberg, D. W., Jr. and D. E. Koshland, Jr.  (1986).  S-methyl glutathione synthesis is catalyzed by the cheR methyltransferase in Escherichia coli.  J.  Bacteriol. 165, 958-963.

Terwilliger, T. C., Wang, J. Y. and D. E. Koshland, Jr.  (1986).  Surface structure recognized for covalent modification of the aspartate receptor in chemotaxis.  Proc. Natl. Acad. Sci.  USA 83, 6707-6710.

Terwilliger, T. C., Kim, S.-H., and D. Eisenberg.  (1987).  Generalized method of determining heavy-atom positions using the difference Patterson function.  Acta Crystallographica  A43, 1-5.  (162 citations).

Terwilliger, T. C. and D. Eisenberg.  (1987).  Isomorphous replacement: effects of errors on the phase probability distribution.  Acta Crystallographica A43, 6-13.

Terwilliger, T. C., Fulford, W. D. and H. B. Zabin.  (1988).  A genetic selection for temperature-sensitive variants of the bacteriophage f1 gene 5 protein.  Nucl. Acids Res.  16, 9027-9039.

Terwilliger, T. C.  (1988).  Construction of a synthetic variant of the bacteriophage f1 gene 5 by assembling oligodeoxynucleotides corresponding to only one strand of DNA.  Gene 61, 41-47.

Terwilliger, T. C.  (1988).  Simple and highly efficient site-specific mutagenesis, by ligation of an oligodeoxyribonucleotide into gapped heteroduplex DNA in which the template strand contains uridine.  Gene 69, 317-324.

Sandberg, W. S. and T. C. Terwilliger  (1989). Influence of interior packing and hydrophobicity on the stability of a protein.  Science 245, 54-57. (137 citations).

Zabin, H., Horvath, M. P. and T. C. Terwilliger  (1991).  Approaches to predicting effects of  single amino acid substitutions on the function of a protein.  Biochemistry 30, 6230- 6240.

Sandberg, W. S. and T. C. Terwilliger  (1991).  Energetics of repacking a protein interior.  Proc. Natl. Acad. Sci. USA 88, 1706-1710.

Sandberg, W. S. and T. C. Terwilliger  (1991).  Repacking Protein Interiors.  Trends in Biotechnology 9, 59-63.

Liang, H. and T. C. Terwilliger  (1991).  Reversible unfolding of the bacteriophage f1 gene 5 protein.  Biochemistry 30, 2772-2782.

Zabin, H. and T. C. Terwilliger  (1991). Isolation and in vitro characterization of temperature- sensitive mutants of the bacteriophage f1 gene V protein.  J. Mol. Biol 219, 257-275.

Sandberg, W. S and T. C. Terwilliger  (1993).  Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl. Acad. Sci. USA 90, 8367-8371.

Liang, H., Sandberg, W. S. and T. C. Terwilliger  (1993). Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding.  Proc. Natl.  Acad. Sci. USA.  90, 7010-7014.

Terwilliger, T. C.  (1994)  MAD phasing: Treatment of dispersive differences as isomorphous replacement information. Acta Crystallographica D50, 17-23.

Terwilliger, T. C. , Zabin, H. B., Horvath, M. P., Sandberg, W. S. and Schlunk, P. M.  (1994) In vivo characterization of mutants of the bacteriophage f1 gene V protein isolated by saturation mutagenesis.  J. Mol. Biol., 236, 556-571.

Terwilliger, T. C.  (1994) MAD phasing: Bayesian estimates of FA .  Acta Crystallographica D50, 11-16.

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).  Structure of the gene V protein of bacteriophage f1 determined by multiwavelength X- ray diffraction on the selenomethionyl protein.  Proc. Natl. Acad. Sci. USA 91, 2071-2075. 

Guan, Y., Zhang, H., Konings, R. N. H., Hilbers, C. W., Terwilliger, T. C., and A. H.- J. Wang  (1994).  Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the gvp-ssDNA complex.  Biochemistry 33, 7768-7778. (20 citations)

Mark, B.L., Terwilliger, T. C., Vaughan, M.R. and Gray, D.M.  (1995).  Circular dichroism spectroscopy of three tryosine-to-phenylalanine substitutions of fd gene 5 protein.  Biochemistry 34, 12854-12865.

Terwilliger, T. C. & Berendzen, J.  (1995).  Difference refinement: Obtaining differences between two related structures.  Acta Crystallographica  D51, 609- 618.

Terwilliger, T. C.  (1995).  Engineering the stability and function of gene V protein.  Advances in Protein Chemistry 46, 177-215.

Sandberg, W.S., Schlunk, P.M., Zabin, H.B., and Terwilliger, T.C.  (1995). Relationship between in vivo activity and in vitro measures of function and stability of a protein.  Biochemistry 34, 11970-11978.

Skinner, M. M. and Terwilliger, T. C.  (1996) An atomic view of additive mutational effects in a protein structure.  Proceedings of the Hanford Symposium on Health and the Environment, 111-121.

Zhang, H., Skinner, M. M., Sandberg, W.S, Wang, A. H.-J., and Terwilliger, T. C.  (1996) Context-dependence of mutational effects in a protein: the crystal structures of the V35I, I47V and V35I/I47V gene V protein core mutants. J. Mol Biol. 259, 148-159.

Cheng, X., Harms, A. C., Goudreau, P.N., Terwilliger, T. C. and Smith, R. D  (1996) Direct Measurement of Oligonucleotide Binding Stoichiometry of Gene V Protein by Mass Spectrometry.  Proc. Natl. Acad. Sci. USA 93, 7022-7027.

Cheng, X., Hofstadler, S. A., Bruce, J. E., Harms, A. C., Chen, R., Smith, R. D., Terwiliger, T. C., and P. N. Goudreau  (1996) Electrospray ionization with high performance Fourier transform ion cyclotron resonance mass spectrometry for the study of noncovalent biomolecular complexes.  Techniques in Protein Chemistry vol. VII. pp. 13-22. Academic Press (San Diego).

Terwilliger, T. C.  (1996) Gene V protein dimerization and cooperativity of binding to poly(dA) Biochemistry, 51, 16652-16664.

Skinner, M. M. and Terwilliger, T. C.  (1996) Potential use of additivity of mutational effects in simplifying protein engineering.  Proc. Natl. Acad. Sci. USA 93, 10753-10757.

Terwilliger, T. C. and Berendzen, J.  (1996).  Bayesian difference refinement.  Acta Crystallographica section D52, 1004-1011.

Terwilliger, T. C. and Berendzen, J.  (1996).  Bayesian weighting for macromolecular crystallographic refinement. Acta Crystallographica D52, 743-748.

Terwilliger, T. C. and Berendzen, J.  (1996).  Correlated phasing of multiple isomorphous replacement data. Acta Crystallographica D52, 749-757.

Benevides, J. M., Terwilliger, T. C., Vhonik, S., and Thomas, G. J., Jr.  (1996).  Raman spectroscopy of the Ff gene V protein and complexes with poly(dA): Non-specific DNA recognition and binding.  Biochemistry, 35, 9603-9609.

Su, S., Gao, Y.-G., Zhang, H., Terwilliger, T. C., and Wang, A. H.-J.  (1997) Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.  Protein Science 6, 771-780.

Terwilliger, T. C. and Berendzen, J.  (1997).  Bayesian correlated MAD phasing.  Acta Crystallographica, D53, 571-579.

Terwilliger, T. C.  (1997). MAD phasing of macromolecular structures: Analysis of MAD data as Single Isomorphous Replacement with Anomalous Scattering (SIRAS) data using the MADMRG program.  Methods in Enzymology 276, 530-537.

Peat T.S., Newman J, Waldo G.S, Berendzen J., Terwilliger T.C.  (1998) Structure Of Translation Initiation-Factor 5a From Pyrobaculum-Aerophilum At 1.75 Angstrom Resolution. Structure 6, 1207-1214.

Thompson, T. M., Mark, B. L., Gray, C. W., Terwilliger, T. C., Sreerama, N., Woody, R. W., Gray, D. M.  (1998).  Circular dichroism and electron microscopy of a core Y61F mutant of the f1 gene 5 single-stranded DNA binding protein, and theoretical analysis of CD spectra of four Tyr-> Phe substitutions.  Biochemistry 37, 7463-7477.

Terwilliger, T. C., Waldo, G., Peat, T. S., Newman, J. M., Chu, K., & Berendzen, J.  (1998).  Class-directed structure determination: Foundation for a Protein Structure Initiative.  Protein Science, 7, 1851-1856.

Ruscetti, T., Newman, J., Peat, T.S., Francis, J., Nolan, R., Terwilliger, T.C., Peterson, S. R., Lehnert, B. E.  (1998). A non-denaturing purification scheme for the DNA binding domain of poly (ADP-ribose) polymerase: a structure-specific DNA binding protein. Protein Expression and Purification, 14, 79-86.

Chen, C.-B., Landgraf, R., Walts, A. D., Chan, L., Schlunk, P. M., Terwilliger, T. C., Sigman, D. S.  (1998). Scission of DNA at a preselected sequence using a single-strand specific chemical nuclease.  Chemistry and Biology 5,283-292.

Terwilliger, T. C. and Berendzen, J.  (1999).  Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methods.  Acta Crystallographica, D55, 501-505.

Terwilliger, T. C. and Berendzen, J.  (1999). Automated MAD and MIR structure solution. Acta Crystallographica, D55, 849-861 (1485 citations)

Terwilliger, T. C.  (1999).Sigma-squared-R, a reciprocal-space measure of the quality of macromolecular electron density maps. Acta Crystallographica, D55, 1174-1178.

Waldo, G., Standish, B. M., Berendzen, J. & Terwilliger, T. C. (1999) Rapid protein-folding assay using green fluorescent protein.  Nature Biotechnology 17, 691-695. (150 citations)

Terwilliger T.C., Berendzen J.  (1999) Exploring structure space: A protein structure initiative. Genetica106, 141-147.

Chang, C.-H., Schindler, J. F., Unkefer, C. J., Vanderberg, L. A., Brainard, J. R., & Terwilliger, T. C.  (1999) In vivo screening of haloalkane dehalogenase mutants.  Chemistry and Biology, 2175-2181.

Terwilliger, T. C. and Berendzen, J.  (1999). Evaluation of macromolecular electron density map quality using the correlation of local rms density. Acta Crystallographica, D55, 1872-1877.

Terwilliger, T. C.  (1999). Reciprocal-space solvent flattening. Acta Crystallographica, D55, 1863-1871

Newman, J., Peat, T. S., Richard, R., Kan, L., Swanson, P. E., Affholter, J. A., Holmes, I. H., Schindler, J. F., Unkefer, C. J., and Terwilliger, T. C. (1999).  Haloalkane dehalogenases: Structure of a Rhodococcus enzyme.  Biochemistry, 38, 16105-16114.

Terwilliger, T. C.  (2000). Maximum-likelihood density modification. Acta Crystallographica, D55, 1863-1871. (404 citations)

Terwilliger, T. C. (2000). Structural Genomics in N. America. Nature Structural Biology 7, 935-939.

Terwilliger, T.C. (2000) Maximum-likelihood density modification for X-ray crystallography. Proceedings of SPIE 4123, 243-248.

Cort, J. R., Mariappan, S. V., Kim, C. Y., Park, M. S., Peat, T. S., Waldo, G. S., Terwilliger, T. C. & Kennedy, M. A. (2001). Solution structure of Pyrobaculum aerophilum DsrC, an archael homologue of the gamma subunit of dissimilatory sulfite reductase. Eur. J. Biochem. 268, 1-10.

Mou, T. C., Gray, C. W., Terwilliger, T. C. & Gray, D. M. (2001). Ff gene 5 protein has a high binding affinity for single-stranded phosphorothioate DNA. Biochemistry 40, 2267-2275.

Terwilliger, T. C. (2001). Maximum likelihood density modification by pattern recognition of structural motifs. Acta Crystallographica D57, 1755-1762.

Terwilliger, T. C. (2001). Map-likelihood phasing. Acta Crystallographica D57, 1763-1775.

Mou, T.-C., Sreerma, N., Terwilliger, T. C., Woody, R. W. & Gray, D. M. (2002). Independent tyrosyl contributions to the CD of Ff gene 5 protein and the distinctive effects of Y41H and Y41F mutants on protein-protein cooperative interaction. Protein Science, 11, 601-613.

Pédelacq, J.-D., Piltch, E., Liong, E. E., Berendzen, J., Kim, C.-Y., Rho, B.-S., Park, M. S., Terwilliger, T. C. & Waldo, G. S (2002). Engineering soluble proteins for structural genomics.  Nature Biotechnology, 20, 927-932.

Goulding, C. W., Apostol, M.,. Anderson, D. H. , Gill, H. S., Smith, C. V., Kuo, M. R., Yang, J. K., Waldo. G. S., Suh, S. W., Chauhan, R., Kale, A., Bachhawat, N., Mande, S. C. , Johnston, J. M., Lott, J. S., Baker, E. N., Arcus, V. L., Leys, D., McLean, K. J., Munro, A. W., Berendzen, J., Sharma, V., Park, M. S., Eisenberg, D.,Sacchettini, J., Alber, T., Rupp. B., Jacobs,W. Jr. and Terwilliger, T. C. (2002). The TB Structural Genomics Consortium: Providing a Foundation for TB Drug Discovery. Current Drug Targets-Infectious Disorders 2, 121-141.

Terwilliger, T. C. (2002) Automated structure solution, density modification, and model-building. Acta Cryst. D58, 1937-1940.

Adams, P. D., McCoy, A. J., Grosse-Kunsteleve, R. W., Hung, L.-W., Ioerger, T. R., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K. & Terwilliger, T. C (2002). PHENIX: Developing new software for automated crystallographic structure determination. Acta Cryst. D Acta Cryst. D58, 1948-1954.

Terwilliger, T. C. (2002). Statistical density modification with non-crystallographic symmetry. Acta Cryst. D58, 2082-2086.

Terwilliger, T. C. (2002). Rapid Automatic NCS identification Using Heavy-Atom Substructures. Acta Cryst. D58, 2213-2215.

Terwilliger, T. C. (2003). Automated main-chain model-building by template-matching and iterative fragment extension. Acta Cryst. D59, 38-44.

Terwilliger, T. C. (2003). Automated side-chain model-building and sequence assignment by template-matching. Acta Cryst. D59, 45-49.

Terwilliger, T. C. (2003). Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement. Acta Cryst. D59, 1174-1182.

Chaudhuri, B. N., Sawaya, M. R., Kim, C.-Y., Waldo, G. S., Park, M. S., Terwilliger, T. C. & Todd O. Yeates, T. O. The Crystal Structure of the First Enzyme in the Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase, from M. tuberculosis (2003).   Structure, 11, 753-764

Terwilliger, T. C., Park, M. S., Waldo, G. S., Berendzen, J., Hung, L.-W., Kim, C.-Y., Smith, C. V., Sacchettini, J. C., Bellinzoni, J., Bossi, R., De Rossi, E., Mattevi, A., Milano, A., Riccardi, G., Rizzi, M., Roberts, M. M., Coker, A. R., Fossati, G., Mascagni, P., Coates, A. R. M., Wood, S. P., Goulding, C. W., Apostol, M., Anderson, D. H., Gill, H. S., Eisenberg, D. S., Taneja, B., Mande, S., Pohl, E., Lamzin, V., Tucker, P., Wilmanns, M., Colovos, C., Meyer-Klaucke, W., Munro, A. W., McLean, KI. J., Marshall, K. R., Leys, D., Yang, J. K., Yoon, H.-J., Lee, B. I., Lee, M. G., Kwak, J. E., Han, B. W., Lee, J. Y, Baek, S.-H., Suh, S. W., Komen, M. M., Arcus, V. M. L., Baker, E. N., Lott, J. S., Jacobs, W., Jr., Alber, T., Rupp, B. (2003). The TB Structural Genomics Consortium: A resource for TB biology. Tuberculosis 83, 223-249.

Terwilliger, T. C. (2003). SOLVE and RESOLVE: Automated structure solution and density modification.  Methods Enzymol.  374, 22-36

Weeks, C. M., Adams, P. D., Berendzen, J., Brunger, A. T., Dodson, E. J., Grosse-Kunstleve, R. W., Schneider, T. R., Sheldrick, G. M., Terwilliger, T. C., and Turkenburg, M. (2003). Automatic solution of heavy-atom substructures.  Methods Enzymol. 374, 37-82.

Mou, T. C.,  Shen, M. C.,  Terwilliger, T. C. Gray, D. M. (2003) Binding and reversible denaturation of double-stranded DNA by Ff gene 5 protein. Biopolymers 70, 637-648.

Terwilliger, T. C. (2003). Statistical density modification using local pattern matching. Acta Cryst. D59, 1688-1701.

Terwilliger, T. C. (2004). SOLVE and RESOLVE: Automated structure solution, density modification, and model building.  J. Synchrotron Rad.  11, 49-52.

Adams, P. D., Gopal, K., Grosse-Kunsteleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Pai, R. K., Read, R. J., Romo, T. D., Sacchettini, J. C., Sauter, N. K., Storoni, L. C. and Terwilliger, T. C. (2004). Recent developments in the PHENIX software for automated crystallographic structure determination.  J. Synchrotron Rad.  11, 53-55.

Kantardjieff, K. A., Kim, C.-Y., Naranjo, G., Waldo, G. S, Lekin, T., Segelke, B. W., Zemla, A., Park, M. S., Terwilliger, T. C. and Rupp, B. (2004). Mycobacterium tuberculosis rmlC epimerase (Rv3465): a promising drug-target structure in the rhamnose pathway.  Acta Cryst. D60, 895-902.

Wang, J. W., Chen, J. R., Gu, Y. X., Zheng, C. D., Jiang, F., Fan, H. F., Terwilliger, T.C., Hao, Q. (2004).  SAD phasing by combination of direct methods with the SOLVE/RESOLVE procedure.  Acta Cryst. D60, 1244-1253.

Terwilliger, T. C. (2004) Structures and technology for biologists. Nature Structural and Molecular Biology 11, 296-297.

Terwilliger, T. C. (2004) Using prime-and-switch phasing to reduce model bias in molecular replacement. Acta Cryst. D60, 2144-2149

Cabantous, S., Terwilliger, T. C., Waldo, G. S. (2005). Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nature Biotechnology 23, 102-107.

Kantardjieff, K.A.; Vasquez, C., Castro, P., Warfel, N.M., Rho, B.S., Lekin, T., Kim, C.Y., Segelke, B.W., Terwilliger, T.C., Rupp, B.  (2005). Structure of pyrR (Rv1379) from Mycobacterium tuberculosis: a persistence gene and protein drug target. Acta Cryst D 61, 355-364.

Pedelacq, J.D., Waldo, G.S., Cabantous, S., Liong, E.C, Terwilliger, T.C. (2005). Structural and functional features of an NDP kinase from the hyperthermophile crenarchaeon Pyrobaculum aerophilum. Protein Science 14, 2562-2573.

Cabantous, S, Pédelacq, J.-D., Mark, B. L., Naranjo, C., Terwilliger, T.C., Waldo, G.S. (2005). Recent Advances in GFP Folding Reporter and Split-GFP Solubility Reporter Technologies. Application to Improving the Folding and Solubility of Recalcitrant Proteins from Mycobacterium tuberculosis.  J. Struct. Func. Genomics 6, 113-119.

Pédelacq, J.-D., Cabantous, S., Tran, T., Terwilliger, T.C., Waldo, G. S. (2006). Engineering and characterization of a superfolder green fluorescent protein. Nature Biotechnology, 24, 79-88.

Furnham, N., Blundell, T. L., DePristo, M. A., Terwilliger, T.C. (2006). Is one solution good enough? Nature Structural & Molecular Biology 13, 184 – 185.

Pédelacq, J.D., Rho, B. S., Kim, C.-Y., Waldo, G. S.,  Lekin, T. P., Segelke, B. W., Rupp, B., Hung, L.-W., Kim, S.-I., Terwilliger, T. C. (2006) Crystal structure of a putative pyridoxine 5'-phosphate oxidase (Rv2607) from Mycobacterium tuberculosis. Proteins. 62:563-569.

Prabu, J. R., Thamotharan, S., Khanduja, J. S., Alipio, E. Z., Kim, C.-Y., Waldo, G.S., Terwilliger, T. C., Segelke, B., Lekin, T., Toppani, D., Hung, L.-W., Yu, M., Bursey, E., Muniyappa, K., Chandara, N.R., Vijayan, M. (2006). Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. Acta Cryst F62, 731-734.

Buchko, G. W., Kim, C.–Y., Terwilliger, T. C., Kennedy, M. A. (2006). Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis. J. Bacteriol. 188, 5993-6001.

Patents issued

Wise, A. A., Kuske, C. R., Terwilliger, T. C. (2004). Detection of phenols using engineered bacteria. US Patent No. 6,773,918 

Terwilliger, T. C. (2004). Maximum likelihood density modification by pattern recognition of structural motifs. US Patent No. 6,721,664.

Terwilliger, T. C.(2005). Likelihood-based modification of experimental crystal structure electron density maps. US Patent No. 6,931,329.

Terwilliger, T. C. (2006) . Method for removing atomic-model bias in macromolecular crystallography. US Patent No. 7,085,653

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