1.11.1.5	?	x * 34418, mass spectrometry	724372	
1.11.1.5	?	x ? 78000, calculated, mature protein, x * 80000, SDS-PAGE	673536	
1.11.1.5	dimer	-	705165	
1.11.1.5	dimer	2 * 36500, SDS-PAGE	-, 394632	
1.11.1.5	dimer	2 * 37500, SDS-PAGE	394626	
1.11.1.5	dimer	2 * 44000, SDS-PAGE	394635	
1.11.1.5	dimer	in the presence of Ca2+, sedimentation equilibrium analysis	657977	
1.11.1.5	dimer	SDS-PAGE, wild type and W191F mutant enzymes	659521	
1.11.1.5	dimer	the dimer is stabilized by hydrophobic interactions between both C-terminal coiled coils of the two monomers. There are also hydrophobic interactions among residues 39-66. The presence of Ca2+ triggers conformational changes, which contribute to stronger interactions within the dimer	660523	
1.11.1.5	dimer	ultracentrifugation, untreated enzyme	659522	
1.11.1.5	heterodimer	SDS-PAGE, H2O2 oxidation induces heterodimerization between cytochrome c and both wild-type and W191F enzymes, but not with W51F mutant	659521	
1.11.1.5	homodimer	2 * 37500, dihemic subunits	687816	
1.11.1.5	homodimer	crystal analysis	664002	
1.11.1.5	monomer	1 * 32500, SDS-PAGE	394611	
1.11.1.5	monomer	with no addition of Ca2+, the monomer/dimer ratio is shifted toward the monomeric form, sedimentation equilibrium analysis	657977	
1.11.1.5	monomer or dimer	the enzyme exhibits a monomer-dimer equilibrium that is dependent not only on the presence of calcium ions but also on pH, ionic strength, and protein concentration	-, 685251	
1.11.1.5	additional information	CcpA three-dimensional structure analysis, overview	724008	
1.11.1.5	additional information	dimerization of wild-type enzyme is observed at H2O2/enzyme ratios of 3 and 10. W191F mutant dimerizes irrespectively of the H2O2/enzyme ratio. W51F mutant exhibits extensive dimerization on H2O2 oxidation and formation of higher molecular weight polymeric species indicating nonspecific crosslinking	659521	
1.11.1.5	additional information	expression of two protein after induction of the enzyme expression, 45000 Da and 47000 Da, SDS-PAGE. The 45000 Da protein is solubilized in 0.1% sodium deoxycholate, which indicates that the protein is only loosely associated with the membrane. The 47000 Da protein is probably initially synthesized with a signal peptide that is later cleaved	657830	
1.11.1.5	additional information	in the presence of added Ca2+ or higher protein concentrations, the enzyme partially shifts to a higher state of aggregation, presumably tetramer	659522	
1.11.1.5	additional information	pair of dimers related by local dyads. Functional dimers can dimerize	657453	
1.11.1.5	additional information	recombinant His-tagged enzyme is used for structure analysis by multidimensional NMR spectroscopy, structure modeling, overview	724372	
1.11.1.5	additional information	three-dimensional structure of MacA by molecular replacement, model building, overview	-, 724337	
1.11.1.5	polymer	SDS-PAGE, W51F mutant	659521	
1.11.1.5	trimer	SDS-PAGE, W51F mutant	659521