THE CONSTRUCT (RESIDUES 30-382) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG ...THE CONSTRUCT (RESIDUES 30-382) WAS EXPRESSED WITH AN N-TERMINAL 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: 3.59 Å3/Da / 溶媒含有率: 65.78 %
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: 6.3 詳細: 20.0% polyethylene glycol 3350, 0.2M ammonium nitrate, No Buffer pH 6.3, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
タイプ: MARMOSAIC 325 mm CCD / 検出器: CCD / 日付: 2009年7月7日 詳細: Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (ho rizontal focusing)
放射
モノクロメーター: single crystal Si(111) bent / 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: 0.97874 Å / 相対比: 1
反射
解像度: 2.46→29.656 Å / Num. obs: 40478 / % possible obs: 99.1 % / 冗長度: 4.2 % / Rmerge(I) obs: 0.094 / Rsym value: 0.094 / Net I/σ(I): 12.1
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
2.46-2.52
4.2
0.811
0.9
12540
2977
0.811
98.7
2.52-2.59
4.2
0.664
1.2
12105
2873
0.664
98.9
2.59-2.67
4.2
0.562
1.3
11943
2835
0.562
98.8
2.67-2.75
4.2
0.427
1.8
11476
2726
0.427
98.8
2.75-2.84
4.2
0.374
2
11078
2635
0.374
98.8
2.84-2.94
4.2
0.289
2.6
10911
2593
0.289
98.9
2.94-3.05
4.2
0.218
3.5
10404
2467
0.218
98.8
3.05-3.18
4.2
0.162
4.7
10063
2401
0.162
99.4
3.18-3.32
4.2
0.126
6
9663
2294
0.126
99.3
3.32-3.48
4.2
0.095
7.7
9159
2185
0.095
99.4
3.48-3.67
4.2
0.081
8.9
8948
2130
0.081
99.1
3.67-3.89
4.2
0.069
6.8
8179
1957
0.069
99.6
3.89-4.16
4.2
0.059
10.5
7835
1874
0.059
99.4
4.16-4.49
4.2
0.049
13.1
7282
1746
0.049
99.7
4.49-4.92
4.2
0.045
14.4
6744
1622
0.045
99.7
4.92-5.5
4.1
0.048
13.8
6023
1453
0.048
99.8
5.5-6.35
4.1
0.056
12
5375
1298
0.056
99.9
6.35-7.78
4.1
0.052
12.9
4495
1096
0.052
100
7.78-11
4
0.047
13
3440
854
0.047
99.9
11-29.661
3.8
0.043
14
1748
462
0.043
94.7
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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
MolProbity
3beta29
モデル構築
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
SCALA
3.2.5
データスケーリング
REFMAC
5.5.0110
精密化
MOSFLM
データ削減
SHELXD
位相決定
精密化
構造決定の手法: 単波長異常分散 / 解像度: 2.46→29.656 Å / Cor.coef. Fo:Fc: 0.913 / Cor.coef. Fo:Fc free: 0.903 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 13.866 / SU ML: 0.173 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R Free: 0.207 立体化学のターゲット値: MAXIMUM LIKELIHOOD WITH PHASES 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED OTHER REFINEMENT REMARKS: 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. SODIUM IONS MODELED ARE PRESENT IN PROTEIN BUFFER. 4. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 5. RESIDUES (A0-A124 AND B0-B122) WERE DISORDERED AND NOT INCLUDED IN THE FINAL MODEL. 6. TLS GROUPS WERE ASSIGNED WITH THE AID OF THE TLSMD SERVER.
Rfactor
反射数
%反射
Selection details
Rfree
0.2506
2033
5 %
RANDOM
Rwork
0.2325
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obs
0.2334
40475
99.21 %
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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