1.8.4.2	?	? * 12000, SDS-PAGE	394863	
1.8.4.2	?	? * 25700, SDS-PAGE	394861	
1.8.4.2	?	x * 17000, SDS-PAGE	741551	
1.8.4.2	?	x * 20000, SDS-PAGE	725524	
1.8.4.2	?	x * 26800, SDS-PAGE	-, 765004	
1.8.4.2	?	x * 54500, calculation from nucleotide sequence	659329	
1.8.4.2	dimer	2 * 16000, SDS-PAGE	763028	
1.8.4.2	dimer	2 * 26000, SDS-PAGE	763028	
1.8.4.2	dimer	2 * 41000, SDS-PAGE	394858	
1.8.4.2	dimer	2 * 60000, SDS-PAGE, dimerization after prolonged storage at -20°C, freeze-thawing or heating at 60°C, monomers held together by an intermolecular disulfide bond	394836	
1.8.4.2	dimer	dimerization of COA6 is unaffected by its concentration. The residues in helix 3 of COA6 are likely involved in dimerization. Dimerization is not due to inter-disulfide bonding between cysteine residues of each COA6 monomer. COA6 structure analysis, overview	-, 764441	
1.8.4.2	homodimer	2 * 14000, SDS-PAGE	-, 670797	
1.8.4.2	homodimer	2 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry	-, 670797	
1.8.4.2	homodimer	2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry	-, 670797	
1.8.4.2	monomer	1 * 12000, SDS-PAGE	763028	
1.8.4.2	monomer	1 * 21100	394853	
1.8.4.2	monomer	1 * 60000, SDS-PAGE	394836	
1.8.4.2	monomer	1 * 62500, SDS-PAGE	394838	
1.8.4.2	additional information	formation of an intramolecular disulfide between Cys27 and Cys30 within the CPYC active site of GRX2	763028	
1.8.4.2	additional information	GRX5 can form covalent homodimers through intermolecular disulfide bonds	763028	
1.8.4.2	additional information	GRX6 can form covalent homodimers through intermolecular disulfide bonds	763028	
1.8.4.2	additional information	the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices	-, 765004	
1.8.4.2	trimer	enzyme contains 3 amino-terminal residues, therefore might be composed of 3 polypeptide chains or subunits	394826