THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAINS WHICH FORM A DIMER BASED ON CRYSTAL PACKING ANALYSIS. SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A DIMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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 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: 2.33 Å3/Da / 溶媒含有率: 47.3 %
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: 6.2 詳細: NANODROP, 0.2M NH4I, 20.0% PEG 3350, No Buffer pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K
モノクロメーター: Single crystal Si(111) bent (horizontal focusing) 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: 0.9791 Å / 相対比: 1
反射
解像度: 2.28→28.513 Å / Num. obs: 31807 / % possible obs: 93.7 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 39.305 Å2 / Rmerge(I) obs: 0.043 / Net I/σ(I): 12.23
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
2.28-2.36
0.24
3
3880
2772
1
42.6
2.36-2.46
0.209
3.7
11775
6904
1
99.9
2.46-2.57
0.173
4.5
11097
6475
1
99.8
2.57-2.7
0.143
5.5
10836
6266
1
99.8
2.7-2.87
0.106
7.2
11335
6559
1
99.7
2.87-3.09
0.075
9.9
11334
6496
1
99.7
3.09-3.4
0.049
14.1
11592
6609
1
99.8
3.4-3.89
0.036
18.8
11538
6528
1
99.3
3.89-4.89
0.025
24.2
11610
6486
1
99.1
4.89-28.513
0.021
26.7
11626
6430
1
96.2
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位相決定
位相決定
手法: 単波長異常分散
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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
SOLVE
位相決定
MolProbity
3beta29
モデル構築
XSCALE
データスケーリング
PDB_EXTRACT
3.004
データ抽出
MAR345
CCD
データ収集
XDS
データ削減
精密化
構造決定の手法: 単波長異常分散 / 解像度: 2.31→28.513 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.907 / SU B: 14.21 / SU ML: 0.192 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.373 / ESU R Free: 0.255 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. IODIDE IONS WERE MODELED BASED ON THE CRYSTALLIZATION CONDITIONS AND ANOMALOUS DIFFERENCE FOURIER PEAKS. 5. CHLORIDE, 1,2-ETHANE DIOL AND PEG WERE MODELED BASED ON CRYSTALLIZATION AND CRYOPROTECTION CONDITIONS. 6. THE CIS PEPTIDE BONDS BETWEEN 104-105 ARE SUPPORTED BY DENSITY. 7. AMINO ACID PRO 87 IN CHAIN B IS A RAMACHANDRAN OUTLIER IN A REGION OF ELECTRON DENSITY THAT IS DIFFICULT TO MODEL.
Rfactor
反射数
%反射
Selection details
Rfree
0.253
1613
5.1 %
RANDOM
Rwork
0.194
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-
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obs
0.197
31794
98.43 %
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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: MASK