2005
DOI: 10.1007/s10969-005-6827-0
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New York-Structural GenomiX Research Consortium (NYSGXRC): A Large Scale Center for the Protein Structure Initiative

Abstract: Structural GenomiX, Inc. (SGX), four New York area institutions, and two University of California schools have formed the New York Structural GenomiX Research Consortium (NYSGXRC), an industrial/academic Research Consortium that exploits individual core competencies to support all aspects of the NIH-NIGMS funded Protein Structure Initiative (PSI), including protein family classification and target selection, generation of protein for biophysical analyses, sample preparation for structural studies, structure de… Show more

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Cited by 53 publications
(54 citation statements)
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“…Worse, for the ten sequence positions listed in Table 2, the percentage of partial occupancy of S versus Se seems to be different in each residue. This is an indication of possibility, that the investigated protein 3B40 [18], was not fully SeMet derivatized. Both refinement paths A and B, carried out in this work, did not allow answering the question what atom type, Se or S, is correct in the refined structure.…”
Section: Handling Of Two Different Atom Types Se and S In Refinemenmentioning
confidence: 89%
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“…Worse, for the ten sequence positions listed in Table 2, the percentage of partial occupancy of S versus Se seems to be different in each residue. This is an indication of possibility, that the investigated protein 3B40 [18], was not fully SeMet derivatized. Both refinement paths A and B, carried out in this work, did not allow answering the question what atom type, Se or S, is correct in the refined structure.…”
Section: Handling Of Two Different Atom Types Se and S In Refinemenmentioning
confidence: 89%
“…The publicly available, from the Protein Data Bank, entry 3B40 [18], which is under extensive investigation in this work, is most likely an example of that case. The partial presence of S-Met residues, or, in other words, not complete Se-Met derivatization of the protein, is possible [15].…”
Section: Handling Of Two Different Atom Types Se and S In Refinemenmentioning
confidence: 99%
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“…The Protein Structure Database (PDB) currently contains ~2,200 proteins of unknown function [27]. These proteins tend to be "orphaned" from any further functional analysis because of a complete absence of information to guide a research project [28][29][30][31]. These orphaned proteins are ideal targets for analysis by FAST-NMR.…”
Section: The Fast-nmr Methodsmentioning
confidence: 99%