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. 1985 Jan 1;225(1):167–176. doi: 10.1042/bj2250167

The crystal structure of beta-lactamase from Staphylococcus aureus at 0.5 nm resolution.

J Moult, L Sawyer, O Herzberg, C L Jones, A F Coulson, D W Green, M M Harding, R P Ambler
PMCID: PMC1144565  PMID: 2983660

Abstract

The preparation, crystallization and low-resolution structure determination of beta-lactamase (EC 3.5.2.6, 'penicillinase') from Staphylococcus aureus is described. The enzyme crystallizes in space group I222 with 1 molecule per asymmetric unit and cell dimensions a = 5.45(1), b = 9.39(1) and c = 13.87(2) nm. The structure was determined at 0.5 nm resolution by using phases calculated from (NH4)2Pt(CN)4 and KAu(CN)2 derivatives. The mean figure of merit mean value of m, for the 1106 reflexions used was 0.70. Difference Fourier syntheses for data collected from crystals soaked in platinum D-methionine and in 6-(4-hydroxy-3,5-di-iodobenzamido)penicilloic acid revealed the likely position of the active site of the enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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