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.
-
実験情報
-
実験
実験
手法: X線回折 / 使用した結晶の数: 1
-
試料調製
結晶
マシュー密度: 3.34 Å3/Da / 溶媒含有率: 63.16 % 解説: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R-SYM, 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
0.97925
1
3
0.97876
1
反射
解像度: 1.85→29.488 Å / Num. obs: 84481 / % possible obs: 96.3 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 24.678 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 10.11
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
1.85-1.92
0.729
1.4
32284
16470
1
95.3
1.92-1.99
0.515
1.9
28258
14335
1
96.2
1.99-2.08
0.36
2.7
31099
15755
1
96.4
2.08-2.19
0.263
3.7
31398
15881
1
96.4
2.19-2.33
0.188
5
32044
16161
1
96.4
2.33-2.51
0.138
6.4
31442
15816
1
96.5
2.51-2.76
0.093
9
31165
15669
1
96.6
2.76-3.16
0.055
14
31681
15906
1
96.6
3.16-3.98
0.028
24.4
31637
15872
1
96.7
3.98-29.488
0.021
32.4
31514
15687
1
95.4
-
位相決定
位相決定
手法: 多波長異常分散
-
解析
ソフトウェア
名称
バージョン
分類
NB
REFMAC
5.5.0053
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: 1.85→29.488 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.945 / Occupancy max: 1 / Occupancy min: 0.19 / SU B: 5.633 / SU ML: 0.076 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.114 / ESU R Free: 0.11 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 RECORDS CONTAIN RESIDUAL B FACTORS ONLY 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...詳細: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY 3.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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4.N-CYCLOHEXYL-3-AMINOPROPANESULFONIC ACID (CXS) FROM CRYSTALLIZATION AND ETHYLENE GLYCOL MOLECULES(EDO) FROM CRYOPROTECTANT ARE MODELED IN THE STRUCTURE, RESPECTIVELY.
Rfactor
反射数
%反射
Selection details
Rfree
0.21
4216
5 %
RANDOM
Rwork
0.18
-
-
-
obs
0.181
84428
99 %
-
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: MASK