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

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Abstract
The preparation, crystallization and low-resolution structure determination of .beta.-lactamase (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 .ltbbrac.m.rtbbrac., for the 1106 reflections used was 0.70. Difference Fourier synthesess 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.