The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution. |
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| Authors: | O Dideberg P Charlier J P Wéry P Dehottay J Dusart T Erpicum J M Frère and J M Ghuysen |
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| Institution: | Laboratoire de Cristalographie, Institut de Physique, University of Liège, Belgium. |
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| 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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