THE CONSTRUCT (24-261) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...THE CONSTRUCT (24-261) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
モノクロメーター: double crystal Si(111) / 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: 0.97951 Å / 相対比: 1
反射
解像度: 1.5→29.212 Å / Num. obs: 91355 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / 冗長度: 3.796 % / Biso Wilson estimate: 18.883 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.059 / Rrim(I) all: 0.069 / Net I/σ(I): 12.12 / Num. measured all: 662500
反射 シェル
解像度 (Å)
Rmerge F obs
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. possible
Num. unique obs
Rrim(I) all
Diffraction-ID
% possible all
1.5-1.55
0.585
0.8
1.8
59447
16354
16232
0.936
1
99.3
1.55-1.62
0.732
0.6
2.4
74169
19687
19670
0.7
99.9
1.62-1.69
0.844
0.423
3.4
62723
16577
16559
0.493
99.9
1.69-1.78
0.924
0.275
5
66897
17603
17592
0.321
99.9
1.78-1.89
0.971
0.173
7.4
65562
17177
17164
0.201
99.9
1.89-2.04
0.988
0.105
11.6
68556
17939
17922
0.122
99.9
2.04-2.24
0.993
0.072
16
64911
16999
16982
0.083
99.9
2.24-2.56
0.996
0.058
19.3
66438
17336
17302
0.067
99.8
2.56-3.23
0.997
0.044
24.2
67811
17687
17636
0.051
99.7
3.23-29.212
0.998
0.034
30.1
65986
17556
17463
0.04
99.5
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位相決定
位相決定
手法: 単波長異常分散
-
解析
ソフトウェア
名称
バージョン
分類
PDB_EXTRACT
3.1
データ抽出
SHELX
位相決定
SHARP
位相決定
XDS
データ削減
XSCALE
November3, 2014BUILT=20141118
データスケーリング
BUSTER
2.10.2
精密化
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: 1.5→29.212 Å / Cor.coef. Fo:Fc: 0.9645 / Cor.coef. Fo:Fc free: 0.9585 / Occupancy max: 1 / Occupancy min: 0.19 / 交差検証法: THROUGHOUT / σ(F): 0 詳細: 1. 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 ...詳細: 1. 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. 2. THE SAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 3. CAPS (CXS), CL, SO4 AND EDO MODELED WERE PRESENT IN PROTEIN/CRYSTALLIZATION CONDITIONS.