SEQUENCE THIS CONSTRUCT (RESIDUES 21-361) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. ...SEQUENCE THIS CONSTRUCT (RESIDUES 21-361) 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: Single crystal Si(111) bent monochromator (horizontal focusing) 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: 0.97852 Å / 相対比: 1
反射
解像度: 2.05→29.748 Å / Num. obs: 35437 / % possible obs: 99.9 % / 冗長度: 7.6 % / Biso Wilson estimate: 37.035 Å2 / Rmerge(I) obs: 0.091 / Rsym value: 0.091 / Net I/σ(I): 16.7
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
2.05-2.1
5.1
0.748
1.8
13038
2571
0.748
99.9
2.1-2.16
5.1
0.654
2
12757
2511
0.654
100
2.16-2.22
5.1
0.534
2.5
12398
2437
0.534
99.9
2.22-2.29
5.1
0.42
3.3
12293
2408
0.42
100
2.29-2.37
5.1
0.349
4
11673
2300
0.349
100
2.37-2.45
5.1
0.288
4.8
11485
2245
0.288
100
2.45-2.54
5.2
0.233
6.1
11088
2152
0.233
100
2.54-2.65
5.2
0.184
7.8
10928
2117
0.184
100
2.65-2.76
8.2
0.23
10.6
16322
1999
0.23
100
2.76-2.9
10.8
0.212
13.9
20692
1910
0.212
100
2.9-3.06
10.9
0.158
18.7
20170
1850
0.158
100
3.06-3.24
10.9
0.12
24.3
18698
1717
0.12
100
3.24-3.47
10.9
0.096
30.5
17780
1630
0.096
100
3.47-3.74
10.8
0.079
37.3
16718
1543
0.079
100
3.74-4.1
10.8
0.069
43.3
15412
1427
0.069
100
4.1-4.58
10.7
0.065
48.4
13574
1267
0.065
100
4.58-5.29
10.5
0.067
48.6
12031
1147
0.067
100
5.29-6.48
10.3
0.066
47.7
10085
983
0.066
100
6.48-9.17
9.9
0.061
50.1
7636
775
0.061
100
9.17-29.75
8.9
0.058
51.9
3969
448
0.058
97.3
-
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
REFMAC
5.5.0053
精密化
PHENIX
精密化
SHELX
位相決定
MolProbity
3beta29
モデル構築
SCALA
3.2.5
データスケーリング
PDB_EXTRACT
3.006
データ抽出
MOSFLM
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: 単波長異常分散 / 解像度: 2.05→29.748 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.959 / Occupancy max: 1 / Occupancy min: 0.35 / SU B: 6.232 / SU ML: 0.079 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.126 / ESU R Free: 0.121 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 RECORD CONTAINS 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 RECORD CONTAINS 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. CALCIUM (CA) AND CACODYLATE (CAC) IONS FROM THE CRYSTALLIZATION SOLUTIONS HAVE BEEN MODELED INTO THE SOLVENT STRUCTURE BASED ON ANOMALOUS DIFFERENCE FOURIERS AND COORDINATION GEOMETRY. 5. ACETATE (ACT) AND FRAMGMENTS OF POLYETHYLENE GLYCOL (PEG and P6G) FROM THE CRYSTALLIZATION/CRYOPROTECTANT SOLUTIONS HAVE BEEN MODELED INTO THE SOLVENT STRUCTURE. 6. TLS GROUPS WERE ASSIGNED WITH THE AID OF THE TLSMD SERVER.
Rfactor
反射数
%反射
Selection details
Rfree
0.191
1773
5 %
RANDOM
Rwork
0.159
-
-
-
obs
0.16
35400
99.91 %
-
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: 1.4 Å / 溶媒モデル: MASK