SEQUENCE THE CONSTRUCT (RESIDUES 31-270) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. ...SEQUENCE THE CONSTRUCT (RESIDUES 31-270) 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: 2.44 Å3/Da / 溶媒含有率: 49.66 %
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: 8.5 詳細: 0.2000M Na2Ci, 30.0000% PEG-400, 0.1M TRIS pH 8.5, 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
0.97905
1
3
0.97839
1
反射
解像度: 1.59→29.311 Å / Num. obs: 107246 / % possible obs: 96.6 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 23.046 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 16.59
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
1.59-1.65
0.01
1.8
168302
22016
1
98.5
1.65-1.71
0.01
2.4
145715
18967
1
98.3
1.71-1.79
0.01
3.3
165731
21445
1
98
1.79-1.88
0.01
5.4
154635
19888
1
97.7
1.88-2
0.01
8.6
166248
21241
1
97.4
2-2.16
0.01
14.1
168089
21332
1
97
2.16-2.37
0.01
20.7
157745
19844
1
96.4
2.37-2.72
0.01
26.6
167281
20838
1
95.8
2.72-3.42
0.01
37.1
160939
19945
1
94.7
3.42-29.311
0.01
48.3
160882
19770
1
92.3
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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
5.2.0019
精密化
PHENIX
精密化
SHELX
位相決定
MolProbity
3beta29
モデル構築
XSCALE
データスケーリング
PDB_EXTRACT
3.006
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: 1.59→29.311 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.966 / Occupancy max: 1 / Occupancy min: 0.25 / SU B: 2.875 / SU ML: 0.051 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.078 / ESU R Free: 0.074 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. 4.2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (TRS) FROM THE CRYSTALLIZATION SOLUTION WAS USED AS A BUFFER. ELECTRON DENSITY WAS POOR FOR SOME REGIONS OF THE STRUCTURE INCLUDING PORTIONS OF THE N-TERMINI, RESIDUES B91-B95, AND C88-C95 THEREFORE, THESE REGIONS WERE NOT MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.185
5379
5 %
RANDOM
Rwork
0.17
-
-
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obs
0.17
107212
96.62 %
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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: BABINET MODEL WITH MASK