Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: an application of reverse screening.
X-ray quality crystals of class I-deoxyribose-5-phosphate aldolase from Escherichia coli have been obtained for the unliganded enzyme and in complex with its substrate, 2-deoxyribose-5-phosphate. The enzyme catalyzes the reversible cleavage of 2-deoxyribose-5-phosphate to acetaldehyde and D-glyceraldehyde-3-phosphate. The unliganded and complex crystals are prismatic long rods and belong to the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 183.1 A, b = 61.4 A, c = 49.3 A and a = 179.2 A, b = 60.5, A, c = 49.1 A, respectively. Two molecules in the asymmetric unit are related by a noncrystallographic 2-fold axis. The crystals are stable in the X-ray beam and diffract to at least 2.6 A. A new method, reverse screening, designed to minimize protein utilization during the screening process was used to determine supersaturation and crystallization conditions.
Stura
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Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA.
Ghosh
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Garcia-Junceda
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Chen
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Wong
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Wilson
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D000446:Aldehyde-Lyases / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology*; D008027:Light; D012267:Ribosemonophosphates / Q000737:chemistry* / Q000378:metabolism; D012542:Scattering, Radiation
D012267:Ribosemonophosphates; C058245:2-deoxyribose 5-phosphate; D000446:Aldehyde-Lyases; C020019:deoxyribose-phosphate aldolase