THE CONSTRUCT (21-605) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...THE CONSTRUCT (21-605) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
モノクロメーター: double crystal Si(111) / プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.97923 Å / 相対比: 1
反射
解像度: 1.59→28.599 Å / Num. obs: 81860 / % possible obs: 97.5 % / Observed criterion σ(I): -3 / 冗長度: 3.2 % / Biso Wilson estimate: 21.531 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.043 / Rrim(I) all: 0.052 / Net I/σ(I): 14.68 / Num. measured all: 514757
反射 シェル
解像度 (Å)
最高解像度 (Å)
Rmerge F obs
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. possible
Num. unique obs
Rrim(I) all
Diffraction-ID
% possible all
1.59-1.65
0.769
0.576
2
54189
17399
16765
0.691
1
96.4
1.65-1.71
0.855
0.418
2.7
46827
14977
14498
0.501
96.8
1.71-1.79
0.921
0.301
3.7
53303
16960
16484
0.361
97.2
1.79-1.88
0.965
0.193
5.7
50041
15815
15447
0.231
97.7
1.88-2
0.984
0.127
8.4
53243
16876
16478
0.152
97.6
2-2.16
0.992
0.082
12.5
53973
17091
16752
0.098
98
2.16-2.37
0.996
0.057
17.2
50125
16027
15734
0.068
98.2
2.37-2.72
0.997
0.042
22.7
52429
16885
16609
0.051
98.4
2.72-3.42
0.998
0.03
31
50193
16389
16027
0.036
97.8
3.42
0.999
0.023
40.2
50434
16608
16058
0.027
96.7
-
位相決定
位相決定
手法: 単波長異常分散
-
解析
ソフトウェア
名称
バージョン
分類
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
XSCALE
November3, 2014BUILT=20141118
データスケーリング
REFMAC
5.8.0103
精密化
SHELXD
位相決定
XDS
データ削減
精密化
構造決定の手法: 単波長異常分散 / 解像度: 1.59→28.599 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.967 / Occupancy max: 1 / Occupancy min: 0.15 / SU B: 3.623 / SU ML: 0.061 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.077 / ESU R Free: 0.075 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: 1. 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 ...詳細: 1. 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. 2. THE SAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. CONDITIONS. 3. EDO MODELED ARE PRESENT IN CRYO CONDITION. 4. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U FACTORS.
Rfactor
反射数
%反射
Selection details
Rfree
0.1752
4082
5 %
RANDOM
Rwork
0.1515
77756
-
-
obs
0.1526
81838
97.65 %
-
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