CRYSTAL PACKING AND ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY ANALYSES SUPPORT THE ASSIGNMENT OF A DIMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
THIS CONSTRUCT (22-154) WAS EXPRESSED WITH THE PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...THIS CONSTRUCT (22-154) WAS EXPRESSED WITH THE 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
0.97805
1
3
0.97862
1
反射
解像度: 1.45→27.077 Å / Num. obs: 39881 / % possible obs: 98.5 % / 冗長度: 2.2 % / Biso Wilson estimate: 13.881 Å2 / Rmerge(I) obs: 0.065 / Rsym value: 0.065 / Net I/σ(I): 9.8
反射 シェル
Diffraction-ID: 1 / 冗長度: 2.2 %
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.45-1.49
0.354
2.1
6406
2872
0.354
97
1.49-1.53
0.302
2.4
6280
2815
0.302
97.5
1.53-1.57
0.249
2.9
6182
2774
0.249
97.7
1.57-1.62
0.213
3.5
6048
2701
0.213
97.8
1.62-1.67
0.185
3.9
5853
2622
0.185
98.4
1.67-1.73
0.155
4.7
5658
2538
0.155
98.1
1.73-1.8
0.135
5.2
5458
2446
0.135
98.6
1.8-1.87
0.113
6.1
5268
2361
0.113
98.5
1.87-1.96
0.1
6.7
5100
2276
0.1
99
1.96-2.05
0.079
8.2
4818
2155
0.079
98.8
2.05-2.16
0.077
8.6
4679
2095
0.077
99.3
2.16-2.29
0.07
8.8
4451
1987
0.07
99.2
2.29-2.45
0.066
9.2
4091
1828
0.066
99.4
2.45-2.65
0.06
10.7
3882
1740
0.06
99.4
2.65-2.9
0.055
11.3
3554
1591
0.055
99.5
2.9-3.24
0.049
12.6
3229
1455
0.049
99.7
3.24-3.74
0.045
12.9
2821
1263
0.045
99.2
3.74-4.59
0.044
13.9
2384
1071
0.044
99.3
4.59-6.48
0.048
12.6
1874
841
0.048
98.8
6.48-27.08
0.053
12
1005
450
0.053
95.5
-
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
5.5.0102
精密化
PHENIX
精密化
SOLVE
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
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.45→27.077 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.961 / Occupancy max: 1 / Occupancy min: 0.15 / SU B: 2.513 / SU ML: 0.043 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.069 / ESU R Free: 0.07 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 RECORD CONTAINS 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 RECORD CONTAINS 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. BICINE (BCN) AND GLYCEROL (GOL) FROM THE CRYSTALLIZATION/ CRYOPROTECTANT SOLUTIONS HAVE BEEN MODELED INTO THE SOLVENT STRUCTURE. 5. THE ELECTRON DENSITY FOR RESIDUES B119-B122 IS POOR. 6. THE CONFORMATION OF THE N-TERMINAL RESIDUES PRECEDING ASN-34 DIFFER CONSIDERABLY BETWEEN THE TWO NCS-RELATED PROTOMERS.
Rfactor
反射数
%反射
Selection details
Rfree
0.182
2004
5 %
RANDOM
Rwork
0.152
-
-
-
obs
0.153
39881
98.25 %
-
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: 1.4 Å / 溶媒モデル: MASK