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The Joint Center for Structural Genomics: a multi-tiered approach to structural genomics

Year: 2005

Type: article

Abstract: MACROMOLECULES C257obtained and 6 structures were determined.Among them, Bs139 protein functions as phosphoribosylglycinamide formyltransferase (GART), an important enzyme in the de novo pathway of purine biosynthesis.Bs139 crystal diffracted to 2.5 Å resolution at home Xray source and the structure was determined by molecular replacement (MR).Bs154 protein is a putative deoxyuridine 5'-triphosphate nucleotidehydrolase (dUTPase), which plays important role in DNA replication.Se-YosS crystal diffraction datasets were collected at Beijing Synchrotron Radiation Facility (BSRF) and the structure was determined by multi-wavelength anomalous diffraction (MAD) method.

Source: Acta Crystallographica Section A Foundations of Crystallography

DOI: 10.1107/s0108767305089014

Authors: M. A. Elsliger, A. M. Deacon, A. Godzik, P. Kuhn, S. A. Lesley, R. C. Stevens, K. O. Hodgson, J. Wooley, I. A. Wilson

Institutions: Scripps Research Institute, Argonne National Laboratory, Joint Center for Structural Genomics, University of Chicago, Stanford Synchrotron Radiation Lightsource, San Diego Supercomputer Center, Genomics Institute of the Novartis Research Foundation, University of California San Diego

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

OpenAlex ID: W2086452371

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