THE CONSTRUCT (RESIDUES 20-400) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 20-400) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
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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: 2.57 Å3/Da / 溶媒含有率: 52.08 %
結晶化
温度: 277 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 6.5 詳細: 1.600000000M NaCitrate, No Buffer pH 6.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
モノクロメーター: Single crystal Si(111) bent monochromator (horizontal focusing) プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.9787 Å / 相対比: 1
反射
解像度: 1.6→29.137 Å / Num. obs: 60601 / % possible obs: 100 % / 冗長度: 3.7 % / Biso Wilson estimate: 12.658 Å2 / Rsym value: 0.126
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位相決定
位相決定
手法: 単波長異常分散
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解析
ソフトウェア
名称
バージョン
分類
NB
REFMAC
5.5.0110
精密化
PHENIX
精密化
SOLVE
位相決定
MolProbity
3beta29
モデル構築
SCALA
3.3.15
データスケーリング
PDB_EXTRACT
3.006
データ抽出
MOSFLM
データ削減
精密化
構造決定の手法: 単波長異常分散 / 解像度: 1.6→29.137 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.958 / Occupancy max: 1 / Occupancy min: 0.2 / SU B: 1.307 / SU ML: 0.045 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R Free: 0.072 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED ...詳細: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 2. CITRATE (CIT), SODIUM (NA) AND GLYCEROL (GOL) MODELED ARE PRESENT IN CRYSTALLIZATION/CRYO CONDITIONS. 3. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
反射数
%反射
Selection details
Rfree
0.175
3058
5.1 %
RANDOM
Rwork
0.144
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obs
0.145
60532
99.94 %
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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