Crystal structure of O‐acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 Å resolution

Andreas Heine, Jaume M. Canaves, Frank von Delft, Linda S. Brinen, Xiaoping Dai, Ashley M. Deacon, Marc A. Elsliger, Said Eshaghi, Ross Floyd, Adam Godzik, Carina Grittini, Slawomir K. Grzechnik, Chittibabu Guda, Lukasz Jaroszewski, Cathy Karlak, Heath E. Klock, Eric Koesema, John S. Kovarik, Andreas Kreusch, Peter Kuhn, Scott A. Lesley, Daniel McMullan, Timothy M. McPhillips, Mark A. Miller, Mitchell D. Miller, Andrew Morse, Kin Moy, Jie Ouyang, Rebecca Page, Alyssa Robb, Kevin Rodrigues, Robert Schwarzenbacher, Thomas L. Selby, Glen Spraggon, Raymond C. Stevens, Henry van den Bedem, Jeff Velasquez, Juli Vincent, Xianhong Wang, Bill West, Guenter Wolf, Keith O. Hodgson, John Wooley, and Ian A. Wilson* The Joint Center for Structural Genomics, Stanford Synchrotron Radiation Laboratory, Stanford University, Menlo Park, California The Genomics Institute of the Novartis Research Foundation, San Diego, California The San Diego Supercomputer Center, La Jolla, California The University of California, San Diego, La Jolla, California The Scripps Research Institute, La Jolla, California

[1]  Peter Kuhn,et al.  Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines. , 2002, Journal of synchrotron radiation.

[2]  Adam Godzik,et al.  Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[3]  Earl W. Cornell,et al.  An approach to rapid protein crystallization using nanodroplets , 2002 .

[4]  P. Burkhard,et al.  Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. , 1999, Journal of molecular biology.

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

[6]  Russ Miller,et al.  The design and implementation of SnB version 2.0 , 1999 .

[7]  D. Job,et al.  Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants--structural and kinetic properties of the free and bound enzymes. , 1998, European journal of biochemistry.

[8]  C. Sander,et al.  Dali: a network tool for protein structure comparison. , 1995, Trends in biochemical sciences.

[9]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

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

[11]  J. Thornton,et al.  PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .

[12]  P. Cook,et al.  Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers. , 1978, The Journal of biological chemistry.

[13]  S. Yamagata.  O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure. , 1976, Journal of biochemistry.

[14]  山縣 修造.  O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast , 1975 .