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Crystallization and preliminary crystallographic data onEscherichia coliTEM1 β-lactamase

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
223
Issue
1
Identifiers
DOI: 10.1016/0022-2836(92)90739-7
Keywords
  • Crystallization
  • β-Lactamase
  • Escherichia Colitem1
  • Antibiotics
  • X-Ray Structure
Disciplines
  • Design

Abstract

Abstract Two crystal forms of Gram − bacteria TEM β-lactamase have been obtained. The tetragonal form has a very large unit cell and diffracts to 3·0 Å resolution. Orthorhombic crystals, grown using ammonium sulfate and a small amount of acetone as precipitating agents, belong to space group P2 12 12 1 with cell parameters a = 43·1 A ̊ , b = 64·4 A ̊ , c = 91·2 a ̊ and diffract to 1·7 Å resolution. A seeding procedure has been designed that ensures reproducibility of the crystal properties. Molecular replacement, using a model reconstructed from the C α co-ordinates from Staphylococcus aureus PC1 β-lactamase, gives a solution that satisfies crystal packing constraints.

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