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 GLY 0 FOLLOWED BY RESIDUES 32-386 OF 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: 0.97907 Å / 相対比: 1
反射
解像度: 1.7→28.97 Å / Num. all: 42521 / Num. obs: 42521 / % possible obs: 100 % / 冗長度: 14.2 % / Biso Wilson estimate: 17.622 Å2 / Rsym value: 0.124 / Net I/σ(I): 14.4
反射 シェル
Diffraction-ID: 1
解像度 (Å)
冗長度 (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.7-1.74
12.9
0.892
0.9
39430
3047
0.892
100
1.74-1.79
14.4
0.7
1.1
43142
2989
0.7
100
1.79-1.84
14.4
0.57
1.4
42244
2930
0.57
100
1.84-1.9
14.4
0.451
1.7
41063
2846
0.451
100
1.9-1.96
14.5
0.35
2.2
39792
2748
0.35
100
1.96-2.03
14.5
0.292
2.6
38817
2684
0.292
100
2.03-2.11
14.4
0.242
3.2
37131
2575
0.242
100
2.11-2.19
14.5
0.201
3.8
35872
2480
0.201
100
2.19-2.29
14.5
0.182
4.1
34717
2401
0.182
100
2.29-2.4
14.4
0.161
4.6
32923
2285
0.161
100
2.4-2.53
14.4
0.14
5.2
31708
2204
0.14
100
2.53-2.69
14.3
0.127
5.6
30137
2102
0.127
100
2.69-2.87
14.3
0.119
5.7
27932
1956
0.119
100
2.87-3.1
14.2
0.11
6
26198
1839
0.11
100
3.1-3.4
14.2
0.085
7.6
24165
1703
0.085
100
3.4-3.8
14
0.07
8.6
22016
1573
0.07
100
3.8-4.39
13.8
0.063
9.4
19213
1391
0.063
100
4.39-5.38
13.7
0.06
9.7
16380
1199
0.06
100
5.38-7.6
13.1
0.067
9.1
12702
969
0.067
100
7.6-28.97
11.6
0.068
8.1
6934
600
0.068
98.4
-
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
NB
MolProbity
3beta29
モデル構築
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
SCALA
3.3.15
データスケーリング
REFMAC
5.6.0116
精密化
MOSFLM
データ削減
SHELXD
位相決定
精密化
構造決定の手法: 単波長異常分散 / 解像度: 1.7→28.97 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.962 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 2.872 / SU ML: 0.049 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.089 / ESU R Free: 0.084 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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. WATERS WERE EXCLUDED FROM TLS REFINEMENT. 4.MAGNESIUM FROM THE CRYSTALLIZATION AND 1,2-ETHANEDIOL (EDO) USED AS A CRYOPROTECTANT WERE MODELED INTO THE STRUCTURE. 5.UNKNOWN LIGANDS (UNL) WAS MODELED INTO THE PUTATIVE ACTIVE SITE. THE POSITIONINGS OF THE UNL'S ARE SIMILAR TO THE POSITIONING OF FRUCTOSE INTO THE ACTIVE SITE ON A RELATED STRUCTURE, AN INVERTASE FROM SCHWANNOCYMES OCCIDENTALIS (PDB ID 3KF3). 6. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 7. ASN A82 IS A RAMACHANDRAN OUTLIER IN MOLPROBITY EVEN THOUGH ITS POSITIONING IS SUPPORTED BY ELECTRON DENSITY.
Rfactor
反射数
%反射
Selection details
Rfree
0.1718
2138
5 %
RANDOM
Rwork
0.149
-
-
-
obs
0.1502
42405
99.96 %
-
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