THE CONSTRUCT (RESIDUES 28-283) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 28-283) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
解像度: 1.44→28.355 Å / Num. obs: 47272 / % possible obs: 76.7 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 17.141 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 10.02
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
1.44-1.49
0.49
1.8
18658
8307
1
79
1.49-1.55
0.374
2.3
20090
8773
1
81.2
1.55-1.62
0.292
3.1
20179
8668
1
80.4
1.62-1.71
0.205
4.3
21311
9049
1
79.6
1.71-1.81
0.155
5.7
18895
7890
1
78.7
1.81-1.95
0.102
8.5
20599
8458
1
77.4
1.95-2.15
0.068
12.4
20734
8316
1
75.8
2.15-2.46
0.053
16.6
20319
7984
1
73.9
2.46-3.1
0.04
21.2
20371
7744
1
71.7
3.1-28.355
0.03
28.2
20470
7549
1
69.7
-
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
5.2.0019
精密化
PHENIX
精密化
SOLVE
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
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.44→28.355 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.967 / Occupancy max: 1 / Occupancy min: 0.22 / SU B: 2.072 / SU ML: 0.041 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.063 / ESU R Free: 0.068 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. A CITRATE (CIT) MOLECULE IS MODELLED FROM CRYSTALLIZATION CONDITIONS, AND PEG-3000 FRAGMENT FROM CRYSTALLIZATION OR PEG-400 FRAGMENT FROM CRYO CONDITIONS (PEG AND PGE) ARE MODELED. 5. THE NOMINAL RESOLUTION IS 1.55 A WITH 9570 OBSERVED REFLECTIONS BETWEEN 1.55-1.44 A (87.7% COMPLETE FOR THIS SHELL) INCLUDED IN THE REFINEMENT.
Rfactor
反射数
%反射
Selection details
Rfree
0.185
2401
5.1 %
RANDOM
Rwork
0.149
-
-
-
obs
0.151
47252
84.51 %
-
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