SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...SEQUENCE 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: 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
相対比: 1
反射
解像度: 1.4→17.61 Å / Num. obs: 36413 / % possible obs: 83.9 % / 冗長度: 3.4 % / Rmerge(I) obs: 0.069 / Rsym value: 0.069 / Net I/σ(I): 6.3
反射 シェル
Diffraction-ID: 1
解像度 (Å)
% possible obs (%)
冗長度 (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Rsym value
1.4-1.44
35.2
1.2
0.246
3.1
1128
0.246
1.44-1.48
48.6
2.3
0.21
3.5
1506
0.21
1.48-1.52
60.2
2.5
0.176
4.2
1834
0.176
1.52-1.57
73.8
2.7
0.152
4.7
2177
0.152
1.57-1.62
91.8
2.9
0.141
5.1
2606
0.141
1.62-1.67
98.4
3.2
0.132
5.3
2731
0.132
1.67-1.74
98.3
3.7
0.122
5.7
2610
0.122
1.74-1.81
98
3.8
0.113
6.1
2508
0.113
1.81-1.89
97.7
3.8
0.096
7
2423
0.096
1.89-1.98
97.4
3.8
0.086
7.7
2289
0.086
1.98-2.09
97
3.8
0.082
8.1
2172
0.082
2.09-2.21
96.3
3.8
0.077
8.2
2055
0.077
2.21-2.37
96.1
3.9
0.072
8.7
1914
0.072
2.37-2.56
95.3
3.9
0.071
9.1
1776
0.071
2.56-2.8
95
3.9
0.069
9.2
1620
0.069
2.8-3.13
94
3.9
0.064
9.8
1453
0.064
3.13-3.61
93.1
3.9
0.058
10.5
1281
0.058
3.61-4.43
91.9
3.9
0.052
12
1073
0.052
4.43-6.26
90.9
3.9
0.06
10.1
821
0.06
6.26-17.61
85.2
3.7
0.063
10.2
436
0.063
-
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
5.2.0005
精密化
SCALA
データスケーリング
PDB_EXTRACT
1.7
データ抽出
MOSFLM
データ削減
CCP4
(SCALA)
データスケーリング
SHELXD
位相決定
SHARP
位相決定
精密化
構造決定の手法: 単波長異常分散 / 解像度: 1.4→17.61 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.959 / SU B: 1.653 / SU ML: 0.032 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / ESU R: 0.06 / ESU R Free: 0.062 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL SE-MET INCORPORATION. 3. GLYCEROL MOLECULES AND A CHLORIDE ANION FROM THE PROTEIN STORAGE BUFFER HAVE BEEN MODELED INTO THE STRUCTURE. THE CHLORIDE ANION IS IN THE VICINITY OF HIS 31 ON SUBUNIT A AND ITS ASSIGNMENT IS PRELIMINARY. 4. ELECTRON DENSITY AT THE PUTATIVE ACTIVE SITES IN EACH OF THE TWO SUBUNITS IS MODELED AS AN UNKNOWN LIGAND, AND A COMPARISON OF THE ELECTRON DENSITY AT EACH OF THE LIGANDS SUGGESTS THE STRUCTURES OF THE TWO LIGANDS ARE DIFFERENT.
Rfactor
反射数
%反射
Selection details
Rfree
0.174
1836
5 %
RANDOM
Rwork
0.148
-
-
-
all
0.149
-
-
-
obs
0.14921
36399
83.43 %
-
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