Crystallization and preliminary X-ray analysis of vicenisaminyltransferase VinC.
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.
Nango
Eriko
E
Department of Chemistry, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551, Japan.
Minami
Atsushi
A
Kumasaka
Takashi
T
Eguchi
Tadashi
T
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D016695:Glycosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D015394:Molecular Structure; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013302:Streptomyces / Q000201:enzymology / Q000235:genetics; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D016695:Glycosyltransferases