THE CONSTRUCT (RESIDUES 23-317) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 23-317) 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: 3.25 Å3/Da / 溶媒含有率: 62.16 %
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 詳細: 1.4M sodium citrate, 0.1 M HEPES pH 7.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
解像度: 2.2→29.643 Å / Num. obs: 23862 / % possible obs: 99.9 % / 冗長度: 4 % / Biso Wilson estimate: 35.684 Å2 / Rmerge(I) obs: 0.097 / Rsym value: 0.097 / Net I/σ(I): 6.793
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
2.2-2.26
4
0.65
1.2
7014
1745
0.65
100
2.26-2.32
4
0.576
1.4
6758
1682
0.576
100
2.32-2.39
4
0.486
1.6
6584
1644
0.486
100
2.39-2.46
4
0.434
1.8
6419
1596
0.434
100
2.46-2.54
4
0.369
2.1
6241
1554
0.369
100
2.54-2.63
4
0.304
2.5
6020
1505
0.304
100
2.63-2.73
4
0.255
3.1
5815
1446
0.255
100
2.73-2.84
4
0.211
3.7
5594
1403
0.211
100
2.84-2.97
4
0.156
5
5435
1355
0.156
100
2.97-3.11
4
0.122
6.2
5092
1278
0.122
100
3.11-3.28
4
0.096
7.4
4924
1241
0.096
100
3.28-3.48
4
0.079
8.8
4644
1170
0.079
100
3.48-3.72
4
0.066
10.3
4368
1104
0.066
100
3.72-4.02
3.9
0.057
11.3
4051
1029
0.057
100
4.02-4.4
3.9
0.05
13.2
3753
962
0.05
100
4.4-4.92
3.9
0.043
14.8
3398
869
0.043
100
4.92-5.68
3.8
0.049
12.7
2981
781
0.049
99.9
5.68-6.96
3.8
0.059
11.4
2482
660
0.059
99.8
6.96-9.84
3.6
0.051
11.7
1916
536
0.051
99.6
9.84-29.65
3.3
0.042
14.3
990
302
0.042
94.3
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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
5.5.0053
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: 2.2→29.643 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.925 / Occupancy max: 1 / Occupancy min: 0.07 / SU B: 9.773 / SU ML: 0.11 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.188 / ESU R Free: 0.171 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 THE ...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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 4. EDO MODELED IS PRESENT IN CRYO SOLUTION. 5. DENSITY FOR RESIDUES 220-229 ARE POOR.
Rfactor
反射数
%反射
Selection details
Rfree
0.229
1220
5.1 %
RANDOM
Rwork
0.189
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obs
0.191
23827
99.84 %
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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