Preliminary X-ray crystallographic studies on the Helicobacter pylori ABC transporter glutamine-binding protein GlnH.

In this study, GlnH has been expressed in E. coli and purified to > 98% homogeneity. The recombinant protein was folded according to the circular dichroism (CD) analysis and behaved as a monomer in solution. Crystals of GlnH have been grown by the hanging-drop vapour-diffusion method using polyethylene glycol (PEG) 4000 as a precipitating agent. The crystals belonged to the primitive monoclinic space group P21 with unit cell parameters a = 38.67, b = 93.36, c = 64.13 Å, β = 93.72°. A complete X-ray diffraction data set was collected to 1.3 Å resolution from a single crystal using synchrotron radiation. Molecular replacement using this data revealed that the asymmetric unit contains a single molecule. This is a key step towards elucidation of the structural basis of the GlnH function. PMID: 30880323 [PubMed - in process]
Source: Drug Discoveries and Therapeutics - Category: Drugs & Pharmacology Tags: Drug Discov Ther Source Type: research