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. DNA SEQUENCING INDICATES THAT RESIDUE 160 IS ASPARTIC ACID (NOT THREONINE) AND RESIDUE 314 IS GLUTAMIC ACID (NOT LYSINE) IN THE CLONED CONSTRUCT. THE SEQUENCING RESULTS ARE CONSISTENT WITH THE ELECTRON DENSITY AND MASS SPECTROMETRY RESULTS FOR THE EXPRESSED PROTEIN.
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
波長: 1.019976 Å / 相対比: 1
反射
解像度: 2.6→29.778 Å / Num. obs: 52320 / % possible obs: 99.8 % / 冗長度: 5.4 % / Biso Wilson estimate: 59.22 Å2 / Rmerge(I) obs: 0.104 / Rsym value: 0.104 / Net I/σ(I): 6.8
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 obs
Rsym value
% possible all
2.6-2.67
4.9
0.771
1
18694
3831
0.771
100
2.67-2.74
5.4
0.673
1.1
20175
3742
0.673
100
2.74-2.82
5.5
0.516
1.5
20117
3627
0.516
100
2.82-2.91
5.5
0.435
1.7
19575
3538
0.435
100
2.91-3
5.5
0.343
2.2
18852
3425
0.343
100
3-3.11
5.5
0.238
3.2
18320
3315
0.238
100
3.11-3.22
5.5
0.195
3.8
17646
3216
0.195
100
3.22-3.36
5.5
0.158
4.7
16947
3088
0.158
100
3.36-3.51
5.5
0.122
5.9
16237
2960
0.122
100
3.51-3.68
5.5
0.102
7.1
15607
2853
0.102
99.9
3.68-3.88
5.5
0.091
7.8
14788
2691
0.091
100
3.88-4.11
5.5
0.076
9.2
14012
2559
0.076
99.9
4.11-4.39
5.5
0.061
11.2
13128
2405
0.061
99.8
4.39-4.75
5.4
0.054
12.4
12404
2278
0.054
99.7
4.75-5.2
5.4
0.052
13
11197
2066
0.052
99.6
5.2-5.81
5.4
0.052
12.9
10178
1888
0.052
99.6
5.81-6.71
5.3
0.046
14.8
8903
1669
0.046
99.4
6.71-8.22
5.3
0.037
17.8
7535
1427
0.037
99.1
8.22-11.63
5.1
0.03
19.9
5752
1129
0.03
98.7
11.63-29.78
4.6
0.027
21
2811
613
0.027
92.5
-
位相決定
位相決定
手法: 分子置換
-
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
REFMAC
5.2.0005
精密化
SCALA
データスケーリング
PDB_EXTRACT
1.701
データ抽出
MOSFLM
データ削減
CCP4
(SCALA)
データスケーリング
MOLREP
位相決定
精密化
構造決定の手法: 分子置換 開始モデル: pdb entry 1y3tA 解像度: 2.6→29.78 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.942 / SU B: 11.787 / SU ML: 0.128 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.202 / ESU R Free: 0.182 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 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 S-MET INCORPORATION. 3.ANOMALOUS DIFFERENCE MAPS INDICATE THE BINDING OF METAL IONS TO THE PROTEIN. X-RAY FLUORESCENCE MEASUREMENTS INDICATE THESE SITES ARE OCCUPIED PREDOMINANTLY BY FERROUS OR FERRIC CATIONS. EACH SUBUNIT CONTAINS TWO BOUND FE ATOMS. 4.ETHYLENE GLYCOL, USED FOR CRYOPROTECTION, WAS MODELED AS A LIGAND TO ONE OF THE FE ATOMS ON EACH SUBUNIT IN THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. L(+)-TARTRATE ANIONS FROM THE CRYSTALLIZATION WERE MODELED AS LIGANDS TO THE SECOND FE ATOM ON EACH SUBUNIT. 5.ADDITIONAL MOLECULES OF ETHYLENE GLYCOL AND TRIS(HYDROXYMETHYL)AMINOMETHANE WERE MODELED. 6.ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
Rfactor
反射数
%反射
Selection details
Rfree
0.204
2666
5.1 %
RANDOM
Rwork
0.167
-
-
-
obs
0.169
52271
99.64 %
-
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