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Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli
N C Blackwell1, P M Cullis, R A Cooper
1Department of Biochemistry, University of Leicester, Leicester LE1 7RH, England.
Abstract:
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 A, alpha = 85 degrees. The crystals diffract to beyond 1.8 A resolution on a Cu Kalpha rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 1.34 A3 Da-1.
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