THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...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.
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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: 2.36 Å3/Da / 溶媒含有率: 47.94 % 解説: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R-SYM, COMPLETENESS AND .
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: 5 詳細: 0.2000M (NH4)2HCitrate, 20.0000% PEG-3350, No Buffer pH 5.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
解像度: 1.6→28.904 Å / Num. obs: 19510 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / 冗長度: 6.94 % / Biso Wilson estimate: 20.689 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 13.65
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
1.6-1.66
1.036
1.45
13683
3655
1
98
1.66-1.72
0.771
1.92
12033
3187
1
99.3
1.72-1.8
0.546
2.7
13852
3656
1
99.6
1.8-1.9
0.324
4.4
14116
3715
1
99.8
1.9-2.02
0.198
7
13582
3566
1
99.9
2.02-2.17
0.125
10.6
12966
3391
1
99.9
2.17-2.39
0.088
14.4
13879
3621
1
100
2.39-2.73
0.064
19.1
13486
3502
1
100
2.73-3.44
0.035
30.7
13820
3584
1
99.9
3.44-28.904
0.023
43.5
13963
3605
1
99.6
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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
5.2.0019
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: 1.6→28.904 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.958 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 3.281 / SU ML: 0.056 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.08 / ESU R Free: 0.083 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. A CHLORIDE ION, FROM THE PROTEIN BUFFER, AND AN ETHYLENE GLYCOL MOLECULE, FROM THE CRYOPROTECTANT, WERE MODELED IN THE STRUCTURE. 5.ONE UNKNOWN LIGAND IS MODELED NEAR TO RESIDUE 69 AND 96.
Rfactor
反射数
%反射
Selection details
Rfree
0.2
990
5.1 %
RANDOM
Rwork
0.167
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-
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obs
0.169
19433
99.7 %
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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: 1.2 Å / 溶媒モデル: BABINET MODEL WITH MASK