2.7.8.43	purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme EptC, sitting drop vapour diffusion method, mixing of 0.004 ml of 30 mg/ml protein in 25 mM NaCl, 10 mM HEPES, pH 7.5, with 0.001 ml of precipitant solution containing 200 mM diammonium phosphate, 15% w/v PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 2.40-2.80 A resolution, molecular replacement	
2.7.8.43	purified recombinant His6-tagged soluble catalytic domain of LptA, free and selenomethionine-labeled, or in complex with Zn2+ and a truncated form of substrate 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine, X-ray diffraction structure determination and analysis at 1.43-1.78 A resolution, molecular replacement. and modeling	
2.7.8.43	recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.5–8.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution	
2.7.8.43	structure of full-length lipid A phosphoethanolamine transferase, determined to 2.75 A resolution. The structure reveals a helical membrane domain and a periplasmic facing soluble domain. The domains are linked by a helix that runs along the membrane surface interacting with the phospholipid head groups. Two helices located in a periplasmic loop between two transmembrane helices contain conserved charged residues and are implicated in substrate binding	
2.7.8.43	structure of the catalytic domain of ICR.. Catalytic domain dimerization is required for substrate binding. The structure reveals two disulfide bonds (Cys390 to Cys398, Cys448 to Cys456)	
2.7.8.43	structure of the catalytic domain ofMCR1 at 1.32 A resolution. The putative nucleophile for catalysis, threonine 285, is phosphorylated in MCR1 and a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site. Binding sites for the lipid A and phosphatidylethanolamine substrates are not apparent in the MCR1 structure