CONTACTS BETWEEN DIMERS ARE WEAK, BUT GEL FILTRATION EXPERIMENTS SHOW THAT THE PROTEIN IS TETRAMERIC AND THE TETRAMERS FORMED IN THE CRYSTAL ARE EQUIVALENT TO THOSE FOUNDIN A DIFFERENT CRYSTAL OF THIS PROTEIN (WITH DIFFERENT SPACEGROUP).
ENGINEERED RESIDUE IN CHAIN A, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN B, ILE 129 TO VAL ...ENGINEERED RESIDUE IN CHAIN A, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN B, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN C, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN D, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN E, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN F, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN G, ILE 129 TO VAL ENGINEERED RESIDUE IN CHAIN H, ILE 129 TO VAL
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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: 2.77 Å3/Da / 溶媒含有率: 55.2 %
結晶化
pH: 6.5 / 詳細: 1.45 M MGSO4, 20 MM CACL2, 0.1 M MES PH 6.5.
解像度: 2.9→25 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.874 / SU B: 35.798 / SU ML: 0.302 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / ESU R Free: 0.401 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE FINAL STRUCTURE ENCOMPASSES THE ENTIRE POLYPEPTIDE CHAIN FROM RESIDUE 3 IN SUBUNITS D AND E, BUT LACKS THE FOLLOWING RESIDUES IN THE ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE FINAL STRUCTURE ENCOMPASSES THE ENTIRE POLYPEPTIDE CHAIN FROM RESIDUE 3 IN SUBUNITS D AND E, BUT LACKS THE FOLLOWING RESIDUES IN THE OTHER SUBUNITS, 202-211 (A), 202-213 AND 367 (B), 203-211 (G AND C), 176-185 AND 196- 213 (H), 203-213 (F).
Rfactor
反射数
%反射
Selection details
Rfree
0.246
3771
5 %
RANDOM
Rwork
0.197
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obs
0.199
70989
99.2 %
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溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: MASK