THE 36 N-TERMINAL RESIDUES OF THE FULL-LENGTH PROTEIN WERE REMOVED FOR CRYSTALLIZATION PURPOSES. ...THE 36 N-TERMINAL RESIDUES OF THE FULL-LENGTH PROTEIN WERE REMOVED FOR CRYSTALLIZATION PURPOSES. THE N-TERMINAL SEQUENCE 'GAMGSGI' OF THE FINAL PROTEIN STEMS FROM THE EXPRESSION LINKER.
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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: 2.6 Å3/Da / 溶媒含有率: 53.3 % / 解説: NONE
結晶化
温度: 277 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 6 詳細: CRYSTALS OF ATGPA1 WERE GROWN AT 4 DEGREES CELSIUS USING THE HANGING-DROP VAPOR-DIFFUSION METHOD. DROPS CONTAINED 1.5 UL OF PROTEIN SOLUTION (20 MG/ML ATGPA1 IN 25 MM TRIS-HCL, PH 7.4, 5% ...詳細: CRYSTALS OF ATGPA1 WERE GROWN AT 4 DEGREES CELSIUS USING THE HANGING-DROP VAPOR-DIFFUSION METHOD. DROPS CONTAINED 1.5 UL OF PROTEIN SOLUTION (20 MG/ML ATGPA1 IN 25 MM TRIS-HCL, PH 7.4, 5% (V/V) GLYCEROL, 150 MM SODIUM CHLORIDE, 1 MM DTT, 500 UL GTP-GAMMA-S) AND WERE EQUILIBRATED AGAINST 1.5 UL OF 0.3 M MAGNESIUM SULFATE, 0.1 M SODIUM CACODYLATE, PH 6.0, 21% (W/V) PEG 8000. INITIALLY OBTAINED CRYSTALS WERE USED FOR MACROSEEDING. CRYSTALS REACHED THEIR FINAL ROD-SHAPE FORM WITHIN 14 DAYS AFTER MACROSEEDING AND WERE CRYOPROTECTED IN THE MOTHER LIQUOR WITH 8% (V/V) GLYCEROL.
解像度: 2.34→96.03 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.904 / SU B: 14.851 / SU ML: 0.164 / 交差検証法: THROUGHOUT / ESU R: 0.295 / ESU R Free: 0.229 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS
Rfactor
反射数
%反射
Selection details
Rfree
0.25378
1520
2.7 %
RANDOM
Rwork
0.2113
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obs
0.21247
54216
99.89 %
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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: MASK