Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli.
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.
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, England.
N C
NC
Blackwell
P M
PM
Cullis
R A
RA
Cooper
T
T
Izard
D000446:Aldehyde-Lyases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D000446:Aldehyde-Lyases; C021468:2-keto-3-deoxy-D-glucarate aldolase