PMID:9761895
| Citation |
Montoya, G, Svensson, C, Savage, H, Schwenn, JD and Sinning, I (1998) Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli. Acta Crystallogr. D Biol. Crystallogr. 54:281-3 |
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| Abstract |
PAPS reductase from E. coli is involved in sulfur metabolism and catalyses the reduction of phospho-adenylyl-sulfate (PAPS) to sulfite. The protein has been cloned, overexpressed and purified from E. coli. Crystallization experiments resulted in crystals suitable for X-ray diffraction. The crystals belong to the orthorhombic space group C2221 with cell dimensions a = 81.9, b = 97.4, c = 109.5 A, and contain one molecule per asymmetric unit. At cryogenic (100 K) temperatures the crystals diffract to a resolution limit of 2.7 A using a rotating anode and to 2.0 A at a synchrotron source. |
| Links | |
| Keywords |
Crystallization; Crystallography, X-Ray; Data Interpretation, Statistical; Escherichia coli/enzymology; Oxidoreductases/chemistry; Oxidoreductases/isolation & purification |
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