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. 1992 Jan 5;223(1):377-80.
doi: 10.1016/0022-2836(92)90739-7.

Crystallization and preliminary crystallographic data on Escherichia coli TEM1 beta-lactamase

C Jelsch  1 , F Lenfant, J M Masson, J P Samama
Affiliations

Crystallization and preliminary crystallographic data on Escherichia coli TEM1 beta-lactamase

C Jelsch et al. J Mol Biol. .

Abstract

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.

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