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  • Title: Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli.
    Author: Montoya G, Svensson C, Savage H, Schwenn JD, Sinning I.
    Journal: Acta Crystallogr D Biol Crystallogr; 1998 Mar 01; 54(Pt 2):281-3. PubMed ID: 9761895.
    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.
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