Published May 24, 2008 | Version v1
Journal article

Crystallization and preliminary X-ray analysis of vicenisaminyltransferase VinC

  • 1. Department of Chemistry, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551 (Japan)
  • 2. Japan Synchrotron Radiation Research Institute (SPring-8/JASRI), Sayo, Hyogo 679-5198 (Japan)
  • 3. Department of Chemistry and Materials Science, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551 (Japan)

Description

The crystallization of VinC, a glycosyltransferase involved in the biosynthesis of the antitumour antibiotic vicenistatin, is reported. 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 Å 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 Å. The presence of two molecules per asymmetric unit gives a crystal volume per protein weight (VM) of 2.43 Å3 Da−1 and a solvent content of 49.5% by volume

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309108014681; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2496844

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
64
Journal Issue
Pt 6
Journal Page Range
p. 558-560
ISSN
1744-3091
CODEN
ACSFCL

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2008
Notes
PMCID: PMC2496844; PMID: 18540075; PUBLISHER-ID: bo5041; OAI: oai:pubmedcentral.nih.gov:2496844