Crystallization and preliminary X-ray analysis of vicenisaminyltransferase VinC

Eriko Nango, Atsushi Minami, Takashi Kumasaka, Tadashi Eguchi

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)558-560
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number6
DOIs
Publication statusPublished - 2008

Keywords

  • Antibiotics
  • Glycosyltransferases
  • Vicenistatin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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