Open AccessCrystallization and preliminary X‐ray analysis of vicenisaminyltransferase VinC
Author(s) -
Nango Eriko,
Minami Atsushi,
Kumasaka Takashi,
Eguchi Tadashi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108014681
Subject(s) - orthorhombic crystal system , crystallization , crystallography , resolution (logic) , crystal (programming language) , synchrotron radiation , recombinant dna , solvent , materials science , diffraction , x ray crystallography , peg ratio , molecule , chemistry , crystal structure , optics , physics , biochemistry , organic chemistry , artificial intelligence , computer science , programming language , gene , finance , economics
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 I 222, 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 ( V M ) of 2.43 Å 3 Da −1 and a solvent content of 49.5% by volume.