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Crystallization and preliminary X-ray analysis of vicenisaminyltransferase VinC.

ABSTRACT: A recombinant glycosyltransferase, VinC, from Streptomyces halstedii HC34 has been crystallized at 293 K using PEG 3350 as precipitant. The diffraction pattern of the crystal extends to 2.0 A resolution at 100 K using synchrotron radiation at SPring-8. The crystals are orthorhombic and belong to space group I222, with unit-cell parameters a = 98.21, b = 130.39, c = 140.11 A. The presence of two molecules per asymmetric unit gives a crystal volume per protein weight (V(M)) of 2.43 A(3) Da(-1) and a solvent content of 49.5% by volume.

SUBMITTER: Nango E

PROVIDER: S-EPMC2496844 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of vicenisaminyltransferase VinC.

Nango Eriko E Minami Atsushi A Kumasaka Takashi T Eguchi Tadashi T

Acta crystallographica. Section F, Structural biology and crystallization communications 20080524 Pt 6

A recombinant glycosyltransferase, VinC, from Streptomyces halstedii HC34 has been crystallized at 293 K using PEG 3350 as precipitant. The diffraction pattern of the crystal extends to 2.0 A resolution at 100 K using synchrotron radiation at SPring-8. The crystals are orthorhombic and belong to space group I222, with unit-cell parameters a = 98.21, b = 130.39, c = 140.11 A. The presence of two molecules per asymmetric unit gives a crystal volume per protein weight (V(M)) of 2.43 A(3) Da(-1) and ...[more]

PMID: 18540075

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