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apo forms of LpxD in space groups P21 and P4322, to 2.7 and 2.8 A resolution, respectively. The asymmetric unit contains two protein trimers
hanging drop vapor diffusion. Crystallographic analyses of recombinant Chlamydia trachomatis LpxD in complex with UDP-GlcNAc, which represents a fragment of substrate, and fatty acid extracted from the bacterial expression system, apo-structure at 2.7 A resolution, and two structures with bound UDP-N-acetylglucosamine (UDP-GlcNAc) at 2.2 A and 3.1 A resolution
hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful
in complex with three forms of acyl carrier protein. Interactions at the interface optimally position acyl carrier protein for acyl delivery and directly involve the pantetheinyl group
purified recombinant His6-tagged LpxD, hanging drop vapour diffusion, 0.002 ml of 15 mg/ml LpxD in 10 mM Tris pH 8, 500 mM NaCl and 1 mM DTT, with 50 mM uridine diphosphate-N-acetylglucosamine, is mixed with 0.002 ml of 100 mM Tris pH 8.5, 1.5 M lithium sulfate, 20°C, 3-5 days, X-ray diffraction structure determination and analysis at 1.3 A resolution, molecular replacement
Results 1 - 5 of 5