The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution
- 31 July 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 245 (3) , 911-913
- https://doi.org/10.1042/bj2450911
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.This publication has 13 references indexed in Scilit:
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