EC Number |
---|
7.1.2.2 | - |
7.1.2.2 | asymmetric crystal structure of bovine mitochondrial F1 |
7.1.2.2 | by sitting drop method at 23°C, to better than 2.8 A resolution |
7.1.2.2 | catalytic site at the alphaTP-betaTP interface with bound MgADP- in crystal structures represents a catalytic site containing inhibitory MgADP- |
7.1.2.2 | complex F1 deltasigma by micro-batch sreening, to 3.1 A resolution, no crystals obtained with complex F1-wt |
7.1.2.2 | crystal structure of the entire subunit E (a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase) at 3.6 A resolution. The structure reveals an extended S-shaped N-terminal alpha-helix with 112.29 A in length, followed by a globular head group |
7.1.2.2 | crystallographic analysis of subunit E, microbatch method using PEG 4000 as a precipitant |
7.1.2.2 | crystals of BeF3-F1 grown by microdialysis in the presence of BeCl2 and NaF and crystallization buffer without AmP-PNP, solved by molecular replacement to 2.2 A resolution, ADP-F1 crystals grown by microdialysis, AMP-PNP omitted from both the inside and outside buffer, ADP concentration increased to 2 mM in the outside buffer, solved by molecular replacement to 2.85 A resolution |
7.1.2.2 | mutant beta subunit |
7.1.2.2 | nucleotide-free alpha3beta3 subcomplex |