THE CONSTRUCT (RESIDUES 37-182) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 37-182) 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: 3.75 Å3/Da / 溶媒含有率: 67.17 % 解説: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R-SYM, COMPLETENESS AND SIGMA(I)>.
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: 65.0% MPD, 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 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
0.97939
1
2
0.91837
1
3
0.97895
1
反射
解像度: 2.72→29.324 Å / Num. obs: 6928 / % possible obs: 98 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 100.287 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 19.96
反射 シェル
Diffraction-ID: 1
解像度 (Å)
最高解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
2.72-2.82
0.943
1.3
3496
1224
91.3
2.82-2.93
0.548
2.2
3657
1259
99.6
2.93-3.06
0.375
3.1
3650
1256
99.7
3.06-3.22
0.218
5.1
3748
1290
99.8
3.22-3.42
0.091
11.2
3818
1311
99.7
3.42-3.69
0.052
18.6
3800
1306
99.4
3.69-4.06
0.031
28.5
3853
1323
99.8
4.06-4.64
0.024
37.3
3623
1251
99.7
4.64-5.82
0.019
43.4
3747
1300
99.7
5.82
0.018
48.7
3432
1232
92.2
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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
SHELX
位相決定
BUSTER-TNT
BUSTER2.8.0
精密化
XSCALE
データスケーリング
PDB_EXTRACT
3.1
データ抽出
XDS
データ削減
SHELXD
位相決定
autoSHARP
位相決定
BUSTER
2.8.0
精密化
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.72→29.324 Å / Cor.coef. Fo:Fc: 0.9513 / Cor.coef. Fo:Fc free: 0.9377 / Occupancy max: 1 / Occupancy min: 0.75 / 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. PHOSPHATE (PO4) FROM PROTEIN BUFFER ARE MODELED. 3. RAMACHANDRAN OUTLIER A74 IS LOCATED IN A REGION WITH POOR DENSITY.