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. 1987 Aug 1;245(3):911–913. doi: 10.1042/bj2450911

The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.

O Dideberg 1, P Charlier 1, J P Wéry 1, P Dehottay 1, J Dusart 1, T Erpicum 1, J M Frère 1, J M Ghuysen 1
PMCID: PMC1148217  PMID: 3499147

Abstract

The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains.

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Selected References

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