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Crystallization and preliminary X-ray analysis of vicenisaminyltransferase VinC
Eriko Nango1, Atsushi Minami, Takashi Kumasaka
1Department of Chemistry, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551, Japan.
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.
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