解像度: 1.59→29.881 Å / Num. obs: 19931 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 23.628 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 12.05
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
0.725
1.5
13950
3793
1
99.4
1.65-1.71
0.557
2.1
12353
3342
1
99.2
1.71-1.79
0.421
2.7
13761
3688
1
99
1.79-1.88
0.287
4.1
13207
3498
1
99.6
1.88-2
0.178
6.4
14210
3746
1
99.8
2-2.16
0.112
10.1
14428
3789
1
99.6
2.16-2.37
0.097
14.4
15974
3541
1
99.8
2.37-2.72
0.102
18.5
23513
3729
1
99.8
2.72-3.42
0.071
26.5
27794
3632
1
100
3.42-29.881
0.053
33.3
28397
3702
1
99.7
-
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: 1.59→29.881 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.957 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 3.187 / SU ML: 0.058 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.082 / ESU R Free: 0.084 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 ...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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. (3). ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. (4). CL IONS AND PEG 400 FRAGMENTS (1PE AND PEG) FROM CRYSTALLIZATION SOLUTION WERE MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.209
1013
5.1 %
RANDOM
Rwork
0.178
-
-
-
obs
0.179
19865
99.7 %
-
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