Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli

被引：4

作者：

Blackwell, NC ^{[1
]}

Cullis, PM

Cooper, RA

Izard, T

机构：

[1] Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England

[2] Univ Leicester, Dept Chem, Leicester LE1 7RH, Leics, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444999006502

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

2-Dehydro-3-deoxygalactarate (DDG) aldolase (E.C. 4.1.2.20) catalyzes the reversible aldol cleavage of DDG and 2-dehydro-3-deoxyglucarate to pyruvate and tartronic semialdehyde. Rhombohedral crystals of recombinant DDG aldolase from Escherichia coli K-12 were obtained. The crystals belong to space group R32 with unit-cell parameters a = 93 Angstrom, alpha = 85 degrees. The crystals diffract to beyond 1.8 Angstrom resolution on a Cu K alpha rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 1.34 Angstrom(3) Da(-1).

引用

页码：1368 / 1369

页数：2

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