title: Crystallization and preliminary X-ray studies of L-aspartase from Escherichia coli.
abstract: Single crystals of L-aspartate ammonia-lyase (L-aspartase) from Escherichia coli have been obtained by microdialysis at room temperature using polyethylene glycol 3350 and sodium acetate as co-precipitants. The crystals exhibit the symmetry of space group P2(1)2(1)2 with a = 156.5 A, b = 147.6 A, c = 102.5 A and diffract at least to 2.8 A.
authors.affiliation: Department of Chemistry, Pennsylvania State University, University Park 16802.
authors.forename: W
authors.initials: W
authors.lastname: Shi
authors.forename: R
authors.initials: R
authors.lastname: Kidd
authors.forename: F
authors.initials: F
authors.lastname: Giorgianni
authors.forename: J F
authors.initials: JF
authors.lastname: Schindler
authors.forename: R E
authors.initials: RE
authors.lastname: Viola
authors.forename: G K
authors.initials: GK
authors.lastname: Farber
mesh_terms: D001220:Aspartate Ammonia-Lyase / Q000648:ultrastructure*; D001426:Bacterial Proteins / Q000648:ultrastructure; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D001220:Aspartate Ammonia-Lyase