THE CONSTRUCT (21-476) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...THE CONSTRUCT (21-476) 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: 2.85 Å3/Da / 溶媒含有率: 56.87 %
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: 8 詳細: 42.00% Ethanol, 0.0500M magnesium chloride, 0.1M TRIS pH 8.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
モノクロメーター: single crystal Si(111) bent / 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
0.97882
1
2
0.91837
1
反射
解像度: 2.5→48.138 Å / Num. obs: 21215 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / 冗長度: 6.55 % / Biso Wilson estimate: 71.778 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 16.46
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 obs
Num. unique obs
% possible all
2.5-2.57
6.66
1.147
1.58
10286
1544
99.5
2.57-2.64
0.912
2
10187
1525
99.9
2.64-2.71
0.685
2.7
9574
1450
99.7
2.71-2.8
0.551
3.2
8822
1432
99.7
2.8-2.89
0.384
4.5
8992
1383
99.1
2.89-2.99
0.273
6.3
9250
1338
99.9
2.99-3.1
0.205
8.1
8907
1309
99.8
3.1-3.23
0.151
10.7
8449
1250
100
3.23-3.37
0.11
14.3
8142
1203
99.9
3.37-3.54
0.08
18.4
7553
1154
99.7
3.54-3.73
0.062
21.9
6368
1073
98.1
3.73-3.95
0.051
28.1
7196
1039
99.8
3.95-4.23
0.041
32.5
6614
965
100
4.23-4.56
0.036
36
6280
936
99.9
4.56-5
0.036
36.7
5481
843
100
5-5.59
0.045
35.2
4330
750
97.5
5.59-6.46
0.046
38.8
4690
702
99.9
6.46-7.91
0.048
38.9
3682
588
100
7.91-11.18
0.034
42.9
2459
449
97.4
11.18-48.14
0.03
48.2
1660
282
97.6
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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
MolProbity
3beta29
モデル構築
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
XSCALE
July4, 2012
データスケーリング
BUSTER-TNT
2.10.0
精密化
XDS
データ削減
SHELXD
位相決定
BUSTER
2.10.0
精密化
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.5→48.138 Å / Cor.coef. Fo:Fc: 0.9503 / Cor.coef. Fo:Fc free: 0.9336 / Occupancy max: 1 / Occupancy min: 0.2 / 交差検証法: THROUGHOUT / σ(F): 0 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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. MG, MPD, AND EOH MODELED ARE PRESENT IN PROTEIN/CRYO CONDITIONS. 4. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. OTHER REFINEMENT REMARKS: 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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. MG, MPD, AND EOH MODELED ARE PRESENT IN PROTEIN/CRYO CONDITIONS. 4. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT.