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 FOLLOWED BY THE TARGET SEQUENCE.
モノクロメーター: Single crystal Si(111) bent (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
0.91162
1
2
0.97929
1
反射
解像度: 1.44→39.193 Å / Num. obs: 40271 / % possible obs: 77.4 % / Biso Wilson estimate: 25.909 Å2 / Rmerge(I) obs: 0.036 / Net I/σ(I): 14.96
反射 シェル
Diffraction-ID: 1
解像度 (Å)
最高解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique all
% possible all
1.44-1.49
0.467
2.2
3810
1355
27.2
1.49-1.55
0.362
3
5952
2030
39
1.55-1.62
0.27
3.9
8354
2847
55.7
1.62-1.71
0.201
5.2
13321
4498
82.9
1.71-1.81
0.149
6.9
13315
4448
93.2
1.81-1.95
0.088
10.8
14593
4891
94.2
1.95-2.15
0.055
16.1
14803
4966
95.2
2.15-2.46
0.039
21.9
14552
4892
95.2
2.46
0.032
26.2
14540
4918
95.9
-
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
MolProbity
3beta29
モデル構築
SHELX
位相決定
REFMAC
5.2.0019
精密化
XSCALE
データスケーリング
PDB_EXTRACT
2
データ抽出
MAR345
CCD
データ収集
XDS
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: 1.44→39.193 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.959 / SU B: 3.311 / SU ML: 0.059 / TLS residual ADP flag: LIKELY RESIDUAL / 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. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 4. CALCIUM IS MODELED BASED ON CRYSTALLIZATION CONDITIONS AND COORDINATION ENVIRONMENT AND GEOMETRY. THE OCCUPANCIES ARE SET AS 0.5 ACCORDING TO DENSITY. STRUCTURAL HOMOLOGS CONTAIN MAGNESIUM AT THE CORRESPONDING SITES. 5. EDO MOLECULES ARE FROM CRYOPROTECTANT. 6. THE NOMINAL RESOLUTION IS 1.60 A WITH 5615 OBSERVED REFLECTIONS BETWEEN 1.60-1.44 (40.5% COMPLETE FOR THIS SHELL) INCLUDED IN THE REFINEMENT.
Rfactor
反射数
%反射
Selection details
Rfree
0.199
2034
5.1 %
RANDOM
Rwork
0.168
-
-
-
all
0.17
-
-
-
obs
0.17
40270
78.61 %
-
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