THE CONSTRUCT (RESIDUES 1-161) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 1-161) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE 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: 2.36 Å3/Da / 溶媒含有率: 47.86 %
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: 4.5 詳細: 0.2000M Na2HPO4, 20.0000% PEG-3350, No Buffer pH 4.5, 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: MAD / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
ID
波長 (Å)
相対比
1
0.91837
1
2
0.97959
1
3
0.97886
1
反射
解像度: 1.95→28.307 Å / Num. obs: 12340 / % possible obs: 97.8 % / 冗長度: 3.6 % / Biso Wilson estimate: 22.604 Å2 / Rmerge(I) obs: 0.093 / Rsym value: 0.093 / Net I/σ(I): 10.9
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
1.95-2
2.8
0.691
1
2023
729
0.691
80.2
2-2.06
3
0.483
1.5
2412
799
0.483
91
2.06-2.12
3.5
0.373
1.9
3101
894
0.373
98.8
2.12-2.18
3.7
0.339
2.1
3085
831
0.339
100
2.18-2.25
3.7
0.269
2.6
3054
833
0.269
100
2.25-2.33
3.7
0.247
3
2994
807
0.247
100
2.33-2.42
3.7
0.209
3.4
2829
771
0.209
100
2.42-2.52
3.7
0.173
4.2
2736
743
0.173
100
2.52-2.63
3.7
0.151
4.8
2628
711
0.151
100
2.63-2.76
3.7
0.128
5.5
2516
682
0.128
100
2.76-2.91
3.7
0.1
6.8
2459
668
0.1
100
2.91-3.08
3.7
0.082
9
2232
605
0.082
100
3.08-3.3
3.7
0.064
10.9
2129
579
0.064
100
3.3-3.56
3.7
0.054
12.5
2054
560
0.054
100
3.56-3.9
3.7
0.051
12.7
1783
488
0.051
100
3.9-4.36
3.7
0.047
13.2
1711
465
0.047
100
4.36-5.03
3.6
0.042
15.7
1461
401
0.042
100
5.03-6.17
3.6
0.054
12.4
1245
347
0.054
100
6.17-8.72
3.5
0.042
15.5
954
273
0.042
100
8.72-28.31
3.3
0.031
20.3
508
154
0.031
98
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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
SOLVE
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
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.95→28.307 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.928 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 6.888 / SU ML: 0.104 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.159 / ESU R Free: 0.148 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). ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. (3). A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING ...詳細: (1). HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. (2). ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. (3). 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. (4). RAMACHANDRAN OUTLIER OF RESIDUE GLY59 IS SUPPORTED BY ELECTRON DENSITY. (5). RESIDUES 102-105 WERE NOT MODELED DUE TO POOR ELECTRON DENSITY IN THIS REGION. (6). DIMETHYL SULFOXIDE (DMS) MOLECULES FROM THE CRYSTALLIZATION BUFFERS WERE MODELED INTO THE STRUCTURE.
Rfactor
反射数
%反射
Selection details
Rfree
0.218
599
4.9 %
RANDOM
Rwork
0.172
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obs
0.174
12306
97.45 %
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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