ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
SEQUENCE THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...SEQUENCE THIS 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.
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実験情報
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実験
実験
手法: X線回折 / 使用した結晶の数: 1
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試料調製
結晶
マシュー密度: 2.96 Å3/Da / 溶媒含有率: 58.45 % 解説: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R-SYM, COMPLETENESS AND .
解像度: 2.5→29.975 Å / Num. obs: 39646 / % possible obs: 93.7 % / Observed criterion σ(I): -3 / 冗長度: 3.79 % / Biso Wilson estimate: 47.923 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 9.14
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
2.5-2.59
0.438
2
13620
6839
1
85.1
2.59-2.69
0.369
2.5
14491
7146
1
93.5
2.69-2.81
0.284
3.2
14932
7354
1
94.5
2.81-2.96
0.216
4.1
15496
7643
1
94.7
2.96-3.15
0.149
5.7
15671
7727
1
94.6
3.15-3.39
0.106
7.7
15114
7461
1
95.2
3.39-3.73
0.068
11.2
15030
7445
1
94.1
3.73-4.26
0.043
15.6
15069
7471
1
95.1
4.26-5.35
0.04
18.2
15164
7510
1
94.9
5.35-29.975
0.035
20.1
15552
7709
1
95.1
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位相決定
位相決定
手法: 多波長異常分散
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解析
ソフトウェア
名称
バージョン
分類
NB
REFMAC
5.5.0053
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: 2.5→29.975 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.926 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 17.234 / SU ML: 0.171 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.4 / ESU R Free: 0.245 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 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. GLYCEROL (GOL) AND ACETATE (ACT) MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE MODELED. 5. THE LIGAND PYRIDOXAL-5'-PHOSPHATE (PLP) IS MODELED INTO BOTH MONOMERS.
Rfactor
反射数
%反射
Selection details
Rfree
0.221
1986
5 %
RANDOM
Rwork
0.178
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obs
0.181
39646
98.82 %
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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: BABINET MODEL WITH MASK