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- W2071301169 abstract "Three crystalline modifications of the bacterial serine peptidase Streptomyces griseus Protease B have been grown. A 4.5 Å resolution electron density map of one form has been computed from the multiple isomorphous replacement (MIR) phases deduced from two heavy metal derivatives plus the anomalous dispersion effects of one of the derivatives. The crystalline modification used was grown from 0.7–1.0 M KH 2 PO 4 at pH 4.2. These crystals have space group P2 1 2 1 2 and unit cell dimensions of a = 44.15 (5) Å, b = 108.72 (10) Å, and c = 37.28 (5) Å. The crystal asymmetric unit contains a protein mass of approximately 19 000 daltons. The electron density map, mean figure of merit 0.80, clearly shows the molecular boundary; relatively long stretches of extended chain are discernable. The active site has been identified from a difference electron density map computed using the MIR protein phases and the amplitude differences between a crystal of the enzyme inhibited at the active serine in solution by p-iodobenzenesulfonyl fluoride (PIPSYL) and those from a crystal of the native enzyme. In addition to showing the site of the PIPSYL binding, there is an apparent conformational change in which the histidine side chain moves away from the serine residue by approximately 4.3 Å." @default.
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- W2071301169 date "1974-03-01" @default.
- W2071301169 modified "2023-09-26" @default.
- W2071301169 title "The 4.5 Å Resolution Structure of a Bacterial Serine Protease from <i>Streptomyces Griseus</i>" @default.
- W2071301169 doi "https://doi.org/10.1139/o74-034" @default.
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