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 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
解像度: 2.05→29.988 Å / Num. obs: 50845 / % possible obs: 100 % / 冗長度: 3.6 % / Biso Wilson estimate: 30.759 Å2 / Rmerge(I) obs: 0.102 / Rsym value: 0.102 / Net I/σ(I): 8.8
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
3.6
0.758
1.6
13492
3708
0.758
100
2.1-2.16
3.6
0.659
1.8
13078
3608
0.659
100
2.16-2.22
3.6
0.567
2.2
12781
3523
0.567
100
2.22-2.29
3.6
0.465
2.6
12342
3410
0.465
100
2.29-2.37
3.6
0.371
3.2
12186
3348
0.371
100
2.37-2.45
3.6
0.305
3.9
11595
3201
0.305
100
2.45-2.54
3.6
0.257
4.6
11265
3100
0.257
100
2.54-2.65
3.6
0.217
5.5
10937
3017
0.217
100
2.65-2.76
3.6
0.19
6.2
10298
2844
0.19
100
2.76-2.9
3.6
0.16
7.7
9933
2749
0.16
100
2.9-3.06
3.6
0.124
9.7
9549
2651
0.124
100
3.06-3.24
3.6
0.101
12.2
8899
2471
0.101
100
3.24-3.47
3.6
0.083
14.5
8500
2366
0.083
100
3.47-3.74
3.6
0.066
17.1
7862
2189
0.066
100
3.74-4.1
3.6
0.053
20
7241
2022
0.053
100
4.1-4.58
3.6
0.047
22.2
6591
1845
0.047
100
4.58-5.29
3.5
0.057
22.8
5773
1648
0.057
100
5.29-6.48
3.4
0.062
23.4
4796
1396
0.062
100
6.48-9.17
3.4
0.042
26.6
3776
1121
0.042
99.9
9.17-29.99
3.1
0.036
27.4
1966
628
0.036
96.7
-
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
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
SHARP
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 2.05→29.988 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.936 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 11.551 / SU ML: 0.154 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.2 / ESU R Free: 0.174 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. GOL AND SO4 MOLECULES FROM THE CRYSTALLIZATION/CRYO SOLUTION ARE MODELED. 5. RESDIUES 22-23, 62-66, 118-123, 204 IN CHAIN A AND 41-42 IN CHAIN B ARE IN POOR ELECTRON DENSITY REGION.
Rfactor
反射数
%反射
Selection details
Rfree
0.237
2572
5.1 %
RANDOM
Rwork
0.194
-
-
-
obs
0.196
50789
99.94 %
-
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: BABINET MODEL WITH MASK