Crystal structure of V1-ATPase at 3.9 angstrom resolution

Origin of Asymmetry at the Intersubunit Interfaces of V1-ATPase from Thermusthermophilus

1.6M ammonium sulfate, 10%(v/v) dioxane, 100mM MES(pH 6.0), 10mM ADP, 10mM magnesium chloride, 1.0mM alminum nitrate, 1.0mM potassium fluoride, VAPOR DIFFUSION, SITTING DROP, temperature 293K

V-type ATP synthase alpha chain (E.C.3.6.3.14), V-type ATP synthase beta chain (E.C.3.6.3.14), V-type ATP synthase subunit D (E.C.3.6.3.14), V-type ATP synthase subunit F (E.C.3.6.3.14)
ATP SYNTHESIS, HYDROGEN ION TRANSPORT, NUCLEOTIDE-BINDING, Catalytic Domain, Molecular Motor Proteins, Quaternary, Proton-Translocating ATPases, Thermus thermophilus, Vacuolar Proton-Translocating ATPases, Hydrolysis, HYDROLASE