Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima at 2.70 Å resolution reveals a new fold
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Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2006-10, Vol.65 (1), p.243-248 |
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creator | Schwarzenbacher, Robert McMullan, Daniel Krishna, S. Sri Xu, Qingping Miller, Mitchell D. Canaves, Jaume M. Elsliger, Marc-André Floyd, Ross Grzechnik, Slawomir K. Jaroszewski, Lukasz Klock, Heath E. Koesema, Eric Kovarik, John S. Kreusch, Andreas Kuhn, Peter McPhillips, Timothy M. Morse, Andrew T. Quijano, Kevin Spraggon, Glen Stevens, Raymond C. van den Bedem, Henry Wolf, Guenter Hodgson, Keith O. Wooley, John Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. |
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doi_str_mv | 10.1002/prot.21058 |
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subjects | Amino Acid Sequence Bacterial Proteins - chemistry Crystallization Crystallography, X-Ray Molecular Sequence Data Phosphotransferases (Alcohol Group Acceptor) - chemistry Protein Folding Thermotoga maritima - enzymology |
title | Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima at 2.70 Å resolution reveals a new fold |
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