| Literature DB >> 18997340 |
Stephen A McMahon1, Muse Oke, Huanting Liu, Kenneth A Johnson, Lester Carter, Nadia Kadi, Malcolm F White, Gregory L Challis, James H Naismith.
Abstract
AcsD, a type A siderophore synthetase with a molecular weight of 71 140 Da from Pectobacterium chrysanthemi, has been expressed, purified and crystallized at 293 K. The protein crystallized in the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 80.3, b = 95.7, c = 161.1 A, alpha = beta = gamma = 90 degrees . Systematic absences were consistent with space group P2(1)2(1)2(1). A complete data set has been collected to 2.25 A resolution on BM14 at the ESRF. Consideration of the likely solvent content suggested that the asymmetric unit contained two molecules. Gel-filtration experiments indicated that the protein was a dimer, although self-rotation analyses did not detect a convincing twofold symmetry axis in the asymmetric unit. The protein has no convincing sequence match to any known structure and thus solution is likely to require experimental phasing.Entities:
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Year: 2008 PMID: 18997340 PMCID: PMC2581690 DOI: 10.1107/S1744309108032132
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091