Structural characterization of the subunit A mutant F508W of the A-ATP synthase from Pyrococcus horikoshii
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Structural characterization of the subunit A mutant F508W of the A-ATP synthase from Pyrococcus horikoshii Descriptor: (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ACETIC ACID, ... Authors: Tadwal, V.S, Manimekalai, M.S.S, Balakrishna, A.M, Gruber, G. Deposit date: 2011-06-09 Release date: 2012-01-25 Last modified: 2023-11-01 Method: X-RAY DIFFRACTION (2.62 Å) Cite: Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy. Acta Crystallogr.,Sect.F, 67, 2011
创建时间：
2011-06-09
