PMID:7675789

Citation	Stura, EA, Ghosh, S, Garcia-Junceda, E, Chen, L, Wong, CH and Wilson, IA (1995) Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: an application of reverse screening. Proteins 22:67-72
Abstract	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.
Links	PubMed Online version:10.1002/prot.340220110
Keywords	Aldehyde-Lyases/chemistry; Aldehyde-Lyases/metabolism; Crystallization; Crystallography, X-Ray/methods; Escherichia coli/enzymology; Light; Ribosemonophosphates/chemistry; Ribosemonophosphates/metabolism; Scattering, Radiation
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