Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution

Morales-Ríos, E.; Montgomery, M.G.; Leslie, A.G.W.; García-Trejo, J.J.; Walker, J.E.

doi:10.1107/S2053230X15016076

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 2
Crystals of the catalytic dimer of α- and β-subunits of the F-ATPase from P. denitrificans. (a) SDS–PAGE analysis of the F₁Δ∊–ζ inhibited complex (15 µg) used in the crystallization experiment. (b) Crystals after 25 d of growth. The bar represents 100 µm. (c) SDS–PAGE analysis of the washed rhombic crystals [top left in (b)]. The positions of the α- and β-subunits of the enzyme are indicated on the right. (d) Packing of αβ dimers in the crystal lattice. The grey box contains an αβ dimer viewed from three aspects related by rotations of 90°.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 71| Part 10| September 2015| Pages 1309-1317

doi:10.1107/S2053230X15016076

Follow Acta Cryst. F

Search IUCr Journals		doi		Advanced search
Author		volume	page