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: 3.18 Å3/Da / 溶媒含有率: 61.37 %
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: 7 詳細: 0.2000M KThioCyanate, 20.0000% PEG-3350, No Buffer pH 7.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
解像度: 2.65→29.566 Å / Num. obs: 9062 / % possible obs: 99.9 % / 冗長度: 10.4 % / Biso Wilson estimate: 52.835 Å2 / Rmerge(I) obs: 0.155 / Rsym value: 0.155 / Net I/σ(I): 15.8
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
2.65-2.72
10.7
0.809
3.1
6904
645
0.809
100
2.72-2.79
10.6
0.639
3.9
6718
633
0.639
100
2.79-2.87
10.7
0.527
5
6584
614
0.527
100
2.87-2.96
10.8
0.45
5.6
6454
600
0.45
100
2.96-3.06
10.7
0.361
7
6248
585
0.361
100
3.06-3.17
10.6
0.286
8.8
5980
564
0.286
100
3.17-3.29
10.6
0.24
10.3
5835
549
0.24
100
3.29-3.42
10.6
0.194
12.8
5600
529
0.194
100
3.42-3.57
10.5
0.166
15
5332
507
0.166
100
3.57-3.75
10.5
0.126
20.3
5160
492
0.126
100
3.75-3.95
10.4
0.124
20.9
4851
465
0.124
100
3.95-4.19
10.4
0.106
24.5
4631
444
0.106
100
4.19-4.48
10.3
0.089
29.2
4386
427
0.089
100
4.48-4.84
10.2
0.086
29.7
4001
392
0.086
100
4.84-5.3
10.2
0.092
28.6
3705
365
0.092
100
5.3-5.93
10
0.097
24.7
3428
343
0.097
100
5.93-6.84
9.8
0.099
24.6
2967
303
0.099
100
6.84-8.38
9.5
0.075
32.4
2484
261
0.075
100
8.38-11.85
9
0.05
43
1970
219
0.05
100
11.85-29.57
7.9
0.06
38.3
992
125
0.06
94.1
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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: 2.65→29.566 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.924 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 12.332 / SU ML: 0.136 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.251 / ESU R Free: 0.214 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 RECORD CONTAINS RESIDUAL B FACTORS ONLY (4). UNEXPLAINED ELECTRON DENSITIES NEAR RESIDUE 6 IN B CHAIN WERE NOT MODELED. (5). THIOCYANATE (SCN) IONS FROM CRYO SOLUTION WERE MODELED. (6). THE RESIDUES 66-95 IN A AND B CHAINS WERE NOT VISIBLE IN THE ELECTRON DENSITY MAPS AND THEY WERE NOT MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.226
427
4.7 %
RANDOM
Rwork
0.188
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obs
0.19
9041
99.87 %
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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