1.8.1.8	analysis of the X-ray structure at 2.0 A resolution	657677	
1.8.1.8	crystal structure exhibits a classic thioredoxin-glutaredoxin fold comprising three alpha-helices surrounding four antiparallel beta-sheets. The crystal lattice has four monomers in a dimer of dimers arrangement. A cadmium ion is found within the active site of each monomer, and two cadmium ions stabilize the N-terminal tails and dimer interfaces. CoMSH and glutathione bind to the active site of methanoredoxin similar to the binding of glutathione in glutaredoxin	741927	
1.8.1.8	hanging-drop vapour diffusion method	677156	
1.8.1.8	purified recombinant His-tagged enzyme LpdA, hanging drop vapour diffusion method at room temperature, 0.003 ml protein solution containing 25 mg/ml protein, 10 mM HEPES, pH 7.5, mixed with 0.002 ml precipitant solution containing 0.1 M trisodium citrate, pH 5.4-5.8, 2.5-5.0% PEG 6000, 3-7 days depending on the pH, crystallization takes longer at higher pH-value, crystals are immersed in 10% PEG 6000, 100 mM MES, pH 5.75, and 25% glycerol, X-ray diffraction structure determination and analysis at 2.8 A resolution	659424	
1.8.1.8	sitting drop vapor diffusion method, using 10% (w/v) PEG 8000, 100 mM HEPES (pH 7.5), and 8 mM cystin at 20°C	725973	
1.8.1.8	sitting-drop vapor diffusion method, crystals belong to the hexagonal space group P6522 with cell dimensions of a = b = 110.3 and c = 68.5 and with one molecule in the asymmtric unit. The structure is solved by multiple isomorphous replacement including anomalous scattering data. The structure is refined to 1.9 resolution	723101