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
收藏
页码：1368 / 1369
页数：2
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