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Crystallization and preliminary crystallographic data for class I deoxyribose‐5‐phosphate aldolase from Escherichia coli : An Application of Reverse Screening
Author(s) -
Stura Enrico A.,
Ghosh Sutapa,
GarciaJunceda Eduardo,
Chen Lihren,
Wong ChiHuey,
Wilson Ian A.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220110
Subject(s) - aldolase a , crystallography , crystallization , orthorhombic crystal system , deoxyribose , chemistry , stereochemistry , crystal structure , enzyme , biochemistry , organic chemistry , dna
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 P 2 1 2 1 2 1 with cell dimensions a = 183.1 Å, b = 61.4 Å, c = 49.3 Å and a = 179.2 Å, b = 60.5, Å, c = 49.1 Å, respectively. Two molecules in the asymmetric unit are related by a noncrystallo‐graphic 2‐fold axis. The crystals are stable in the X‐ray beam and diffract to at least 2.6 Å. A new method, reverse screening, designed to minimize protein utilization during the screening process was used to determine supersaturation and crystallization conditions. © 1995 Wiley‐Liss, Inc.