1. THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED ...1. 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. 2. THE PROTEIN WAS REDUCTIVELY METHYLATED PRIOR TO CRYSTALLIZATION.
モノクロメーター: Single crystal Si(111) bent monochromator (horizontal focusing) プロトコル: MAD / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
ID
波長 (Å)
相対比
1
0.91837
1
2
0.9786
1
3
0.97806
1
反射
解像度: 1.9→28.904 Å / Num. obs: 34930 / % possible obs: 100 % / 冗長度: 7.4 % / Biso Wilson estimate: 21.874 Å2 / Rmerge(I) obs: 0.137 / Rsym value: 0.137 / Net I/σ(I): 11.9
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
1.9-1.95
7.4
0.986
0.8
18804
2539
0.986
100
1.95-2
7.4
0.781
1
18483
2491
0.781
100
2-2.06
7.4
0.606
1.3
17819
2396
0.606
100
2.06-2.12
7.4
0.513
1.5
17432
2347
0.513
100
2.12-2.19
7.4
0.42
1.8
17031
2294
0.42
100
2.19-2.27
7.5
0.355
2.1
16431
2205
0.355
100
2.27-2.36
7.4
0.304
2.5
15735
2113
0.304
100
2.36-2.45
7.4
0.268
2.8
15360
2072
0.268
100
2.45-2.56
7.5
0.213
3.6
14749
1975
0.213
100
2.56-2.69
7.4
0.18
4.2
14061
1896
0.18
100
2.69-2.83
7.4
0.157
4.8
13379
1804
0.157
100
2.83-3
7.4
0.133
5.5
12642
1710
0.133
100
3-3.21
7.4
0.107
6.6
11820
1598
0.107
100
3.21-3.47
7.3
0.086
4.1
11082
1510
0.086
100
3.47-3.8
7.3
0.066
9.8
10242
1395
0.066
100
3.8-4.25
7.3
0.057
10.5
9232
1271
0.057
100
4.25-4.91
7.2
0.062
10.3
8209
1134
0.062
100
4.91-6.01
7.1
0.07
8.4
6886
967
0.07
100
6.01-8.5
7
0.049
12.4
5313
762
0.049
100
8.5-28.91
6.3
0.048
11.2
2844
451
0.048
97.6
-
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
5.5.0053
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
autoSHARP
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.9→28.904 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.936 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 5.507 / SU ML: 0.072 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.118 / ESU R Free: 0.118 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 THE ...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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 4. POLY ETHYLENE GLYCOL FRAGMENTS (PGE, P6G) MODELED ARE PRESENT IN CRYSTALLIZATION/CRYO CONDITIONS.
Rfactor
反射数
%反射
Selection details
Rfree
0.206
1752
5 %
RANDOM
Rwork
0.167
-
-
-
obs
0.169
34930
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: MASK