SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUGGESTS A HEXAMER AS A OLIGOMERIZATION STATE IN SOLUTION. CRYSTAL PACKING SUPPORTS THE ASSIGNMENT A MONOMER OR DIMER.
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
0.97922
1
3
0.97876
1
反射
解像度: 1.5→29.709 Å / Num. obs: 72017 / % possible obs: 99.4 % / 冗長度: 3.6 % / Biso Wilson estimate: 14.52 Å2 / Rmerge(I) obs: 0.092 / Rsym value: 0.092 / Net I/σ(I): 10
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
1.5-1.54
3.6
0.568
0.9
18540
5189
0.568
98.7
1.54-1.58
3.6
0.44
1.7
18169
5078
0.44
98.8
1.58-1.63
3.6
0.358
2.1
17806
4996
0.358
99
1.63-1.68
3.6
0.313
2.4
17185
4807
0.313
99.1
1.68-1.73
3.6
0.271
2.5
16790
4693
0.271
99.1
1.73-1.79
3.6
0.218
3.4
16338
4548
0.218
99.3
1.79-1.86
3.6
0.18
4.1
15831
4397
0.18
99.5
1.86-1.94
3.6
0.183
1.1
15235
4255
0.183
99.7
1.94-2.02
3.6
0.132
2.7
14854
4095
0.132
99.8
2.02-2.12
3.6
0.126
2.2
14183
3925
0.126
99.6
2.12-2.24
3.7
0.099
6.7
13654
3711
0.099
99.6
2.24-2.37
3.7
0.108
3.4
12873
3525
0.108
99.6
2.37-2.54
3.7
0.085
7.5
12390
3355
0.085
99.9
2.54-2.74
3.7
0.083
5.2
11495
3129
0.083
99.9
2.74-3
3.7
0.068
8.9
10605
2880
0.068
100
3-3.35
3.7
0.062
9.4
9700
2640
0.062
100
3.35-3.87
3.6
0.062
7.3
8494
2337
0.062
100
3.87-4.74
3.6
0.053
11
7209
2005
0.053
99.9
4.74-6.71
3.5
0.055
10.4
5514
1568
0.055
99.6
6.71-29.71
3.3
0.059
9.7
2920
884
0.059
96.3
-
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
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
SHELXD
位相決定
精密化
構造決定の手法: 多波長異常分散 / 解像度: 1.5→29.709 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.962 / Occupancy max: 1 / Occupancy min: 0.2 / SU B: 2.277 / SU ML: 0.046 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.068 / ESU R Free: 0.068 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.NADPH MOLECULEs FROM BACTERIAL NATURAL PROCESSING AND CHLORIDE IONS FROM CRYSTALLIZATION ARE MODELED IN THE STRUCTURE. ETHYLENE GLYCOL MOLECULES FROM CRYOPROTECTANT ARE ALSO MODELED IN THE STRUCTURE.
Rfactor
反射数
%反射
Selection details
Rfree
0.174
3626
5 %
RANDOM
Rwork
0.149
-
-
-
obs
0.15
71950
99.2 %
-
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