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.
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
0.97941
1
3
0.97904
1
反射
解像度: 1.6→28.41 Å / Num. obs: 69473 / % possible obs: 98.3 % / 冗長度: 2.6 % / Biso Wilson estimate: 15.579 Å2 / Rmerge(I) obs: 0.072 / Rsym value: 0.072 / Net I/σ(I): 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
1.6-1.64
2.5
0.444
1.7
12170
4868
0.444
94
1.64-1.69
2.6
0.351
1.6
12739
4956
0.351
97.7
1.69-1.74
2.6
0.307
1.7
12473
4848
0.307
97.7
1.74-1.79
2.6
0.243
3.1
12043
4685
0.243
97.9
1.79-1.85
2.6
0.206
3.6
11780
4575
0.206
98.1
1.85-1.91
2.6
0.16
4.6
11393
4420
0.16
98.2
1.91-1.98
2.6
0.129
5
11023
4282
0.129
98.3
1.98-2.07
2.6
0.113
3.8
10612
4118
0.113
98.5
2.07-2.16
2.6
0.099
7.1
10181
3956
0.099
98.8
2.16-2.26
2.6
0.084
8.3
9814
3812
0.084
98.8
2.26-2.39
2.6
0.075
9
9275
3596
0.075
99
2.39-2.53
2.6
0.069
9.9
8853
3437
0.069
99.1
2.53-2.7
2.6
0.065
10.2
8304
3228
0.065
99.3
2.7-2.92
2.6
0.059
10.7
7754
3010
0.059
99.3
2.92-3.2
2.6
0.053
11.6
7156
2794
0.053
99.6
3.2-3.58
2.6
0.046
13.2
6384
2496
0.046
99.6
3.58-4.13
2.5
0.047
12.3
5651
2221
0.047
99.7
4.13-5.06
2.5
0.041
13.8
4796
1898
0.041
99.6
5.06-7.16
2.5
0.044
13.8
3729
1469
0.044
99.8
7.16-28.41
2.5
0.046
11.9
1983
804
0.046
97.9
-
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
データスケーリング
PDB_EXTRACT
3.004
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: 多波長異常分散 / 解像度: 1.6→28.41 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.959 / SU B: 1.367 / SU ML: 0.049 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.077 / ESU R Free: 0.079 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. ZN IS MODELED BASED ON AN X-RAY FLOURESCENCE SCAN, ANOMALOUS DIFFERENCE FOURIERS, AND COORDINATION GEOMETRY. 4. A SULFATE (SO4) ION, A GLYCEROL (GOL) MOLECULE AND FOUR CHLORIDE IONS ARE MODELED BASED ON CRYSTALLIZATION CONDITIONS, ELECTRON DENSITY AND COORDINATION GEOMETRY.
Rfactor
反射数
%反射
Selection details
Rfree
0.175
3499
5 %
RANDOM
Rwork
0.141
-
-
-
obs
0.142
69445
98.15 %
-
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