CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF WILD-TYPE AND K272A MUTANT GLUTAMATE 1-SEMIALDEHYDE AMINOTRANSFERASE FROM SYNECHOCOCCUS

被引：8

作者：

HENNIG, M ^{[1
]}

GRIMM, B ^{[1
]}

JENNY, M ^{[1
]}

MULLER, R ^{[1
]}

JANSONIUS, JN ^{[1
]}

机构：

[1] INST PLANT GENET & CROP PLANT RES,D-06466 GATERSLEBEN,GERMANY

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 242卷 / 04期

关键词：

CHLOROPHYLL BIOSYNTHESIS; PYRIDOXAL-5'-PHOSPHATE; SITE-DIRECTED MUTAGENESIS; X-RAY DIFFRACTION;

D O I：

10.1006/jmbi.1994.1606

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Crystals of the pyridoxal-5'-phosphate dependent enzyme glutamate-1-semialdehyde aminotransferase (EC 5.4.3.8) from Synechococcus have been grown from polyethylene glycol solutions. The wild type enzyme crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 68.4 Angstrom, b = 108.0 Angstrom, c = 122.6 Angstrom. The inactive mutant in which the cofactor-binding lysine 272 residue is replaced by alanine (K272A) gives monoclinic crystals of space group P2(1) with cell dimensions a = 67.1 Angstrom, b = 108.6 Angstrom, c = 124.5 Angstrom and beta = 115.7 degrees. These crystal forms diffract to 2.4 Angstrom and 2.7 Angstrom resolution, respectively.

引用

页码：591 / 594

页数：4

共 16 条

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