THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...THE CONSTRUCT 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: 2.33 Å3/Da / 溶媒含有率: 47.16 %
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 詳細: 0.2000M Ca(OAc)2, 20.0000% PEG-8000, 0.1M MES pH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
解像度: 1.6→27.875 Å / Num. obs: 40560 / % possible obs: 99.9 % / 冗長度: 3.6 % / Biso Wilson estimate: 14.705 Å2 / Rmerge(I) obs: 0.092 / Rsym value: 0.092 / Net I/σ(I): 5.825
反射 シェル
Diffraction-ID: 1
解像度 (Å)
冗長度 (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.6-1.64
3.6
0.498
1.5
10793
2958
0.498
99.7
1.64-1.69
3.7
0.429
1.7
10489
2873
0.429
99.8
1.69-1.74
3.6
0.346
2.2
10277
2818
0.346
99.9
1.74-1.79
3.6
0.284
2.6
10016
2746
0.284
100
1.79-1.85
3.7
0.237
3.1
9585
2604
0.237
100
1.85-1.91
3.7
0.203
3.7
9407
2566
0.203
100
1.91-1.98
3.7
0.168
4.4
9102
2489
0.168
100
1.98-2.07
3.7
0.132
5.6
8760
2383
0.132
100
2.07-2.16
3.6
0.113
6.5
8443
2315
0.113
100
2.16-2.26
3.7
0.104
7
8024
2182
0.104
100
2.26-2.39
3.7
0.096
7.5
7626
2088
0.096
100
2.39-2.53
3.7
0.087
8
7249
1985
0.087
100
2.53-2.7
3.7
0.086
8
6864
1879
0.086
100
2.7-2.92
3.6
0.074
9.1
6401
1766
0.074
100
2.92-3.2
3.6
0.063
10.2
5810
1613
0.063
100
3.2-3.58
3.6
0.053
10.6
5301
1469
0.053
99.8
3.58-4.13
3.6
0.052
11.4
4686
1316
0.052
99.6
4.13-5.06
3.5
0.057
9.7
3902
1112
0.057
99.5
5.06-7.16
3.4
0.065
9.1
2993
883
0.065
98.9
7.16-27.88
3.1
0.053
10.5
1603
515
0.053
96.4
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位相決定
位相決定
手法: 多波長異常分散
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解析
ソフトウェア
名称
バージョン
分類
NB
REFMAC
5.2.0019
精密化
PHENIX
精密化
SHELX
位相決定
MolProbity
3beta29
モデル構築
SCALA
3.2.5
データスケーリング
PDB_EXTRACT
3.006
データ抽出
MOSFLM
データ削減
SHELXD
位相決定
autoSHARP
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.6→27.875 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.943 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 2.874 / SU ML: 0.052 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.083 / ESU R Free: 0.084 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: (1). HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. (2). A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN ...詳細: (1). HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. (2). 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. (3). ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. (4). ACETATE (ACT) IONS FROM THE CRYSTALLIZATION SOLUTION AND A GLYCEROL (GOL) MOLECULE FROM CRYO SOLUTION WERE MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.198
2031
5 %
RANDOM
Rwork
0.168
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obs
0.169
40506
99.77 %
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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