title: An improved purification of ECF1 and ECF1F0 by using a cytochrome bo-deficient strain of Escherichia coli facilitates crystallization of these complexes.
abstract: A novel strategy, which employs a cytochrome bo-lacking strain (GO104) and a modified isolation procedure provides an effective approach for obtaining much purer preparations of ECF1F0 than described previously, as well as for isolating homogeneous and protein-chemically pure ECF1. ECF1 obtained in this way could be crystallized by vapor-diffusion using polyethylene glycol (PEG) as a precipitant in a form suitable for X-ray diffraction analysis. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with lattice parameters a = 110, h = 134, and c = 269 A, and diffract to a resolution of at least 6.4 A.
authors.affiliation: Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
authors.forename: G
authors.initials: G
authors.lastname: Grüber
authors.forename: A
authors.initials: A
authors.lastname: Hausrath
authors.forename: M
authors.initials: M
authors.lastname: Sagermann
authors.forename: R A
authors.initials: RA
authors.lastname: Capaldi
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D003573:Cytochrome b Group / Q000235:genetics / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D017353:Gene Deletion; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000302:isolation & purification*; D013045:Species Specificity
chemical_list: D003573:Cytochrome b Group; D006180:Proton-Translocating ATPases