Crystallization and preliminary crystallographic data on Escherichia coli TEM1 beta-lactamase.
Two crystal forms of Gram- bacteria TEM beta-lactamase have been obtained. The tetragonal form has a very large unit cell and diffracts to 3.0 A resolution. Orthorhombic crystals, grown using ammonium sulfate and a small amount of acetone as precipitating agents, belong to space group P2(1)2(1)2(1) with cell parameters a = 43.1 A, b = 64.4 A, c = 91.2 A and diffract to 1.7 A resolution. A seeding procedure has been designed that ensures reproducibility of the crystal properties. Molecular replacement, using a model reconstructed from the C alpha co-ordinates from Staphylococcus aureus PC1 beta-lactamase, gives a solution that satisfies crystal packing constraints.
Jelsch
C
C
Laboratoire de Cristallographie Biologique IBMC, 67084 Strasbourg, France.
Lenfant
F
F
Masson
J M
JM
Samama
J P
JP
D001426:Bacterial Proteins / Q000648:ultrastructure; D003461:Crystallography; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D011994:Recombinant Proteins; D014961:X-Ray Diffraction; D001618:beta-Lactamases / Q000648:ultrastructure*
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D001618:beta-Lactamases