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
0.9787
1
3
0.97833
1
反射
解像度: 1.7→29.161 Å / Num. obs: 48232 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 20.057 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 14.75
反射 シェル
解像度 (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
Diffraction-ID
% possible all
1.7-1.76
0.735
1.8
31307
8862
1
98
1.76-1.83
0.55
2.5
32871
9056
1
99.7
1.83-1.91
0.382
3.6
32542
8795
1
99.5
1.91-2.02
0.256
5.4
37255
9923
1
99.7
2.02-2.14
0.178
7.7
33123
8665
1
99.7
2.14-2.31
0.127
10.4
35723
9329
1
99.7
2.31-2.54
0.087
14.8
34889
9054
1
99.7
2.54-2.9
0.062
19.8
34555
8950
1
99.8
2.9-3.66
0.032
33.1
35982
9278
1
99.8
3.66-29.161
0.022
47.7
35536
9139
1
99.4
-
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
XSCALE
データスケーリング
PDB_EXTRACT
3.006
データ抽出
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: 1.7→29.161 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.963 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 2.841 / SU ML: 0.05 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.083 / ESU R Free: 0.082 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 RECORDS CONTAIN 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 RECORDS CONTAIN 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 0.80 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. A FLAVIN MONONUCLEOTIDE (FMN) MOLECULE ARE MODELED INTO THE PUTATIVE ACTIVE SITE ON EACH MONOMER. DURING THE REFINEMENT, THE FMN RESTRAINTS DICTIONARY WAS MODIFIED TO ALLOW BENDING OF THE ISOALLOXAZINE RING ALONG THE N5-N10 VIRTUAL AXIS RESULTING IN AN IMPROVED FIT BETWEEN THE FNN COORDINATES AND ELECTRON DENSITY. 5. AN UNKNOWN LIGAND (UNL) MOLECULE IS MODELED INTO THE PUTATIVE ACTIVE SITE OF EACH MONOMER. EACH UNL IS LOCATED ABOVE THE ISOALLOXAZINE MOIETY OF EACH FMN AND ITS SHAPE IS SIMILAR TO EITHER BENZOATE/NITOBENZENE OR BENZOATE/NITROBENZENE DERIVATIVES. 6. SULFATE (SO4) ION AND ETHYLENE GLYCOL (EDO) ARE MODELED BASED ON CRYSTALLIZATION AND CRYO CONDITION. 7. THERE ARE UNEXPECTED DENSITIES FOUND NEAR G171 AND THESE WERE NOT MODELED.
Rfactor
反射数
%反射
Selection details
Rfree
0.172
2445
5.1 %
RANDOM
Rwork
0.145
-
-
-
obs
0.146
48177
99.72 %
-
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