Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli.
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.
European Molecular Biology Laboratory, Structural Biology Programme, 69117 Heidelberg, Germany.
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Montoya
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Svensson
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Savage
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Schwenn
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Sinning
D003460:Crystallization; D018360:Crystallography, X-Ray; D003627:Data Interpretation, Statistical; D004926:Escherichia coli / Q000201:enzymology*; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification*
D010088:Oxidoreductases; C052449:3'-phosphoadenylyl-5'-phosphosulfate reductase