A: Oxidoreductase, iron/ascorbate family B: Oxidoreductase, iron/ascorbate family C: Oxidoreductase, iron/ascorbate family D: Oxidoreductase, iron/ascorbate family ヘテロ分子
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: 2.24 Å3/Da / 溶媒含有率: 45 % 解説: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R MERGE, COMPLETENESS AND .
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
0.97963
1
3
0.97916
1
反射
解像度: 2.2→29.587 Å / Num. obs: 59238 / % possible obs: 98 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 30.859 Å2 / Rmerge(I) obs: 0.088 / Net I/σ(I): 7.98
反射 シェル
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
Diffraction-ID
% possible all
2.2-2.28
0.522
1.6
20383
10943
1
95.2
2.28-2.37
0.4
2
20341
10834
1
97.2
2.37-2.48
0.332
2.5
21380
11284
1
97.8
2.48-2.61
0.265
3.1
21121
11053
1
98.2
2.61-2.77
0.204
4
20919
10888
1
98.4
2.77-2.98
0.152
5.3
21470
11070
1
98.8
2.98-3.28
0.098
8.1
21894
11245
1
98.9
3.28-3.76
0.056
13.1
22124
11354
1
98.8
3.76-4.72
0.038
18.4
21755
11125
1
99
4.72-29.587
0.031
21.2
22146
11236
1
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
SHELX
位相決定
REFMAC
5.5.0110
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
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.2→29.587 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.919 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 11.31 / SU ML: 0.151 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.301 / ESU R Free: 0.217 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 SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE ...詳細: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 5. 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. 6. CHLORIDE (CL) AND POLYETHYLENE GLYCROL (PEG) FROM THE CRYSTALLIZATION AND GLYCEROL(GOL) USED AS A CRYOPROTECTANT HAVE BEEN MODELED INTO THE STRUCTURE.
Rfactor
反射数
%反射
Selection details
Rfree
0.2345
2982
5 %
RANDOM
Rwork
0.1847
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-
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obs
0.1873
59183
99.53 %
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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: 1.4 Å / 溶媒モデル: MASK