The full-length protein was subjected to limited proteolysis by chymotrypsin right before ...The full-length protein was subjected to limited proteolysis by chymotrypsin right before crystallization. Only ACT domain is present in the structure
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実験情報
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実験
実験
手法: X線回折 / 使用した結晶の数: 1
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試料調製
結晶
マシュー密度: 2.45 Å3/Da / 溶媒含有率: 49.89 %
結晶化
温度: 289 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 8.5 詳細: 0.2 ul of 15 mg/ml protein in 20 mM HEPES pH 7.5, 500 mM NaCl, 5% Glycerol, and 10 mM BME were mixed with 0.2 ul of the MCSG Suite I condition #31 (0.1 M Tris pH=8.5, 0.2 M Calcium chloride, ...詳細: 0.2 ul of 15 mg/ml protein in 20 mM HEPES pH 7.5, 500 mM NaCl, 5% Glycerol, and 10 mM BME were mixed with 0.2 ul of the MCSG Suite I condition #31 (0.1 M Tris pH=8.5, 0.2 M Calcium chloride, 25% w/v PEG 4000) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). Before crystallization protein was incubated with 1/50 v/v of 2 mg/ml chymotrypsin solution at 289 K for 3 hours.
構造決定の手法: 単波長異常分散 / 解像度: 2.01→41.63 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.947 / SU B: 8.848 / SU ML: 0.116 / SU R Cruickshank DPI: 0.1527 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.153 / ESU R Free: 0.157 詳細: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS