ENGINEERED RESIDUE IN CHAIN A, LYS 294 TO ALA ENGINEERED RESIDUE IN CHAIN A, CYS 411 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, LYS 294 TO ALA ENGINEERED RESIDUE IN CHAIN A, CYS 411 TO ALA ENGINEERED RESIDUE IN CHAIN A, ALA 423 TO CYS ENGINEERED RESIDUE IN CHAIN B, LYS 294 TO ALA ENGINEERED RESIDUE IN CHAIN B, CYS 411 TO ALA ENGINEERED RESIDUE IN CHAIN B, ALA 423 TO CYS
配列の詳細
K294A IS AN ENGINEERED MUTATION. C411A AND A423C HAVE ALSO BEEN INTRODUCED TO GIVE HIGHER ...K294A IS AN ENGINEERED MUTATION. C411A AND A423C HAVE ALSO BEEN INTRODUCED TO GIVE HIGHER EXPRESSION. THE PROTEIN WITH THESE TWO MUTATIONS BEHAVES LIKE WILD-TYPE. UNK RESIDUES B 12-27 REPRESENT SECTION OF CHAIN B STRUCTURE WITH NO ASSIGNED SEQUENCE. ACTUAL SEQUENCE OF CHAIN B IS SUPPOSED TO BE IDENTICAL TO CHAIN A, FOR RESIDUES 1-50, SEQUENCE ASSIGNMENT COULD NOT BE DONE IN THE ELECTRON DENSITY DUE TO UNKNOWN REGISTER.
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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: 4
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試料調製
結晶
マシュー密度: 4.3 Å3/Da / 溶媒含有率: 71.4 % / 解説: 5 DATASETS WERE COLLECTED ON 4 CRYSTALS AND MERGED
解像度: 2.73→68.01 Å / Cor.coef. Fo:Fc: 0.8345 / Cor.coef. Fo:Fc free: 0.8639 / 交差検証法: THROUGHOUT / σ(F): 0 詳細: THE ELECTRON DENSITY QUALITY WAS BETTER FOR CHAIN A. CHAIN B WAS BUILT LARGELY WITH CHAIN A AS A MODEL.