THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...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: 2.44 Å3/Da / 溶媒含有率: 49.58 %
結晶化
温度: 277 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 7.1 詳細: NANODROP, 0.20M NaF, 20.0% PEG 3350, No Buffer pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 277K
解像度: 1.75→34.401 Å / Num. obs: 96949 / % possible obs: 96.6 % / 冗長度: 6.5 % / Rmerge(I) obs: 0.097 / Rsym value: 0.097 / Net I/σ(I): 5.515
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
1.75-1.8
1.9
0.396
1.7
9940
5324
0.396
73.9
1.8-1.84
3.7
0.47
1.5
22141
6005
0.47
84.4
1.84-1.9
4.3
0.378
1.9
28384
6642
0.378
95.9
1.9-1.96
5.3
0.305
2.4
35450
6670
0.305
98.9
1.96-2.02
6.3
0.261
2.8
41171
6529
0.261
99.9
2.02-2.09
6.7
0.208
3.5
42419
6376
0.208
99.9
2.09-2.17
6.9
0.18
4
42113
6112
0.18
100
2.17-2.26
7.2
0.154
4.6
42818
5933
0.154
100
2.26-2.36
7.7
0.144
4.8
43445
5663
0.144
100
2.36-2.47
7.7
0.123
5.6
42077
5486
0.123
100
2.47-2.61
7.7
0.109
6.3
39824
5190
0.109
100
2.61-2.77
7.7
0.096
6.9
37882
4926
0.096
100
2.77-2.96
7.7
0.092
6.9
35815
4635
0.092
100
2.96-3.2
7.7
0.084
7.3
33411
4319
0.084
100
3.2-3.5
7.7
0.078
7.6
31237
4040
0.078
100
3.5-3.91
7.7
0.073
8
27985
3636
0.073
100
3.91-4.52
7.7
0.061
9.9
24694
3224
0.061
100
4.52-5.53
7.5
0.064
8.7
20881
2767
0.064
100
5.53-7.83
7.4
0.058
10.9
16232
2192
0.058
100
7.83-34.401
6.8
0.068
6.8
8726
1280
0.068
98.8
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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
SCALA
3.2.5
データスケーリング
PDB_EXTRACT
3.006
データ抽出
MAR345
CCD
データ収集
MOSFLM
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: 1.75→34.401 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.958 / Occupancy max: 1 / Occupancy min: 0.15 / SU B: 4.162 / SU ML: 0.059 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.095 / ESU R Free: 0.094 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. NA AND CL IONS FROM THE PURIFICATION MEDIA ARE MODELED. 5. ETHYLENE GLYCOL MOLECULES FROM THE CRYO SOLUTION ARE MODELED. 6. FRAGMENTS OF PEG 3350 (PE4) MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE MODELED. 7. RESIDUE LYS 259 IS MODELED AS LLP BECAUSE OF ITS COVALENT LINKAGE TO A PYRIDOXAL-5'-PHOSPHATE (PLP) MOLECULE BOUND TO THE PROTEIN.
Rfactor
反射数
%反射
Selection details
Rfree
0.171
4788
5 %
RANDOM
Rwork
0.137
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obs
0.139
96109
95.59 %
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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