CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE FROM ESCHERICHIA-COLI

被引：7

作者：

WEDEKIND, JE

FREY, PA

RAYMENT, I

机构：

[1] UNIV WISCONSIN, COLL AGR & LIFE SCI, GRAD SCH, INST ENZYME RES, MADISON, WI 53705 USA

[2] UNIV WISCONSIN, COLL AGR & LIFE SCI, DEPT BIOCHEM, MADISON, WI 53705 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1994年 / 50卷

关键词：

D O I：

10.1107/S0907444993012958

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Galactose-1-phosphate uridylyltransferase catalyzes the formation of UDP-galactose during normal cellular metabolism, making it an essential enzyme in all cells. The enzyme from Escherichia coli has been crystallized at pH 5.9 in the presence of phenyl-UDP (P1-5'-uridyl-P2-phenyl diphosphate), a substrate analog, using PEG 10000 in combination with Li2SO4 and NaCl. Crystals belong to space group P2(1)2(1)2 with unit-cell dimensions a - 58.6, b - 217.6 and c = 69.6 angstrom. There is one dimer or two subunits in the asymmetric unit. Crystals are relatively insensitive to X-ray radiation and diffract beyond 2.5 angstrom resolution. A low-resolution native data set has been recorded.

引用

页码：329 / 331

页数：3

共 21 条

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