The site-specific incorporation of p-iodo-L-phenylalanine into proteins for structure determination

[1]  Zbigniew Dauter,et al.  Jolly SAD. , 2003, Acta crystallographica. Section D, Biological crystallography.

[2]  Peter G Schultz,et al.  An Expanded Eukaryotic Genetic Code , 2003, Science.

[3]  G. Sheldrick,et al.  In-house measurement of the sulfur anomalous signal and its use for phasing. , 2003, Acta crystallographica. Section D, Biological crystallography.

[4]  P. Schultz,et al.  Addition of the keto functional group to the genetic code of Escherichia coli , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[5]  S. Yokoyama,et al.  Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells. , 2002, Nucleic acids research.

[6]  George M Sheldrick,et al.  Substructure solution with SHELXD. , 2002, Acta crystallographica. Section D, Biological crystallography.

[7]  K. Kirshenbaum,et al.  Biosynthesis of Proteins Incorporating a Versatile Set of Phenylalanine Analogues , 2002, Chembiochem : a European journal of chemical biology.

[8]  T. Terwilliger.  Maximum-likelihood density modification using pattern recognition of structural motifs , 2001, Acta crystallographica. Section D, Biological crystallography.

[9]  P. Schultz,et al.  Expanding the Genetic Code of Escherichia coli , 2001, Science.

[10]  Z Dauter,et al.  Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. , 2000, Acta crystallographica. Section D, Biological crystallography.

[11]  G Bricogne,et al.  Can anomalous signal of sulfur become a tool for solving protein crystal structures? , 1999, Journal of molecular biology.

[12]  Thomas C. Terwilliger,et al.  Automated MAD and MIR structure solution , 1999, Acta crystallographica. Section D, Biological crystallography.

[13]  S. Steinbacher,et al.  Bioincorporation of telluromethionine into proteins: a promising new approach for X-ray structure analysis of proteins. , 1997, Journal of molecular biology.

[14]  G. Murshudov,et al.  Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.

[15]  R M Esnouf,et al.  An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. , 1997, Journal of molecular graphics & modelling.

[16]  D. M. F. Aalten,et al.  PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules , 1996, J. Comput. Aided Mol. Des..

[17]  E A Merritt,et al.  Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.

[18]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[19]  M. Hatada,et al.  Bio–incorporation of telluromethionine into buried residues of dihydrofolate reductase , 1994, Nature Structural Biology.

[20]  B. Matthews,et al.  Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. , 1993, Journal of molecular biology.

[21]  B. Matthews,et al.  Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. , 1991, Biochemistry.

[22]  P. Kraulis.  A program to produce both detailed and schematic plots of protein structures , 1991 .

[23]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[24]  P. Brick,et al.  Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. , 1989, Journal of molecular biology.

[25]  B. Matthews,et al.  Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. , 1987, Journal of molecular biology.

[26]  Wayne A. Hendrickson,et al.  Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur , 1981, Nature.

[27]  G. Thomas,et al.  Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis. , 1999, Trends in cell biology.

[28]  Z. Otwinowski,et al.  Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.

[29]  V S Lamzin,et al.  Automated refinement of protein models. , 1993, Acta crystallographica. Section D, Biological crystallography.

[30]  Z. Dauter,et al.  Biological Crystallography Protein Crystal Structure Solution by Fast Incorporation of Negatively and Positively Charged Anomalous Scatterers , 2022 .