THIS CONSTRUCT (RESIDUES 30-288) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THIS CONSTRUCT (RESIDUES 30-288) 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: 4.02 Å3/Da / 溶媒含有率: 69.43 % 解説: THE STATISTICS REPORTED IN REMARK 200 WERE COMPUTED WITH XSCALE WITH FRIEDEL PAIRS KEPT SEPARATE.
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: 9.1 詳細: 0.200M Na2HPO4, 20.00% PEG-3350, No Buffer, pH 9.1, 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
0.91837
1
2
0.97931
1
3
0.97868
1
反射
解像度: 2.4→28.825 Å / Num. obs: 18955 / % possible obs: 98.1 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 40.298 Å2 / Rmerge(I) obs: 0.195 / Net I/σ(I): 6.88
反射 シェル
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
2.4-2.49
0.979
1.5
13833
3524
94
2.49-2.58
0.846
1.8
12555
3200
98.5
2.58-2.7
0.674
2.2
14339
3645
98.1
2.7-2.84
0.548
2.8
13590
3462
98.6
2.84-3.02
0.419
3.6
14129
3598
98.5
3.02-3.25
0.261
5.6
13706
3488
98.3
3.25-3.58
0.165
8.5
14249
3620
98.8
3.58-4.09
0.103
12.6
13749
3503
98.8
4.09-5.14
0.086
14.6
14077
3579
99
5.14-28.825
0.084
15
14209
3616
98.2
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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
REFMAC
5.5.0102
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: 2.4→28.825 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.932 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 11.169 / SU ML: 0.142 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R Free: 0.191 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 U 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 U 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. 7. POLYETHYLENE GLYCOL-3350 (PEG) FRAGMENTS AND ETHYLENE GLYCOL (EDO) FROM THE CRYSTALLIZATION/CRYOPROTECTION SOLUTION AND A SODIUM ION (NA) FROM THE PROTEIN BUFFER ARE MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.2166
965
5.1 %
RANDOM
Rwork
0.1694
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-
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obs
0.1718
18936
98.26 %
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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: BABINET MODEL WITH MASK