- PDB-2ogy: Asn199Ala Mutant of the 5-methyltetrahydrofolate corrinoid/iron s... -
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データベース: PDB / ID: 2ogy
タイトル
Asn199Ala Mutant of the 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.3 Angstrom resolution
要素
5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase
ジャーナル: J.Biol.Chem. / 年: 2007 タイトル: Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl ...タイトル: Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. 著者: Doukov, T.I. / Hemmi, H. / Drennan, C.L. / Ragsdale, S.W.
温度: 298 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 7.5 詳細: 8-15% PEGMME 5000, 0.05M CALCIUM ACETATE, 20% GLYCEROL, 0.05M HEPES BUFFER; 3-FOLD MOLAR EXCESS OF THE MTHF SUBSTRATE (SCHRICKS LABOLATORIES, JONA, SWITZERLAND). THE SUPERSATURATION OF THE ...詳細: 8-15% PEGMME 5000, 0.05M CALCIUM ACETATE, 20% GLYCEROL, 0.05M HEPES BUFFER; 3-FOLD MOLAR EXCESS OF THE MTHF SUBSTRATE (SCHRICKS LABOLATORIES, JONA, SWITZERLAND). THE SUPERSATURATION OF THE PRECIPITANT SOLUTION REQUIRED DILUTION OF THE PROTEIN-CH3-H4FOLATE COMPLEX BY 50-100-FOLD IN ORDER TO OBTAIN SINGLE CRYSTALS, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K