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Instruments / Technical Area	Publication Details	Published	Actions
I24-Microfocus Macromolecular Crystallography	Cloning, purification and structure determination of the HIV integrase-binding domain of lens epithelium-derived growth factor Clare Hannon , Abimael Cruz-Migoni , Olga Platonova , Robin L. Owen , Joanne E. Nettleship , Ami Miller , Stephen B. Carr , Gemma Harris , Terence H. Rabbitts , Simon E. V. Phillips Acta Crystallographica Section F Structural Biology Communications 74, 143 - 149 DOI: 10.1107/S2053230X18001553 Diamond Proposal Number(s): [12346] Open Access Show Abstract ▼ Abstract: Lens epithelium-derived growth factor (LEDGF)/p75 is the dominant binding partner of HIV-1 integrase in human cells. The crystal structure of the HIV integrase-binding domain (IBD) of LEDGF has been determined in the absence of ligand. IBD was overexpressed in Escherichia coli, purified and crystallized by sitting-drop vapour diffusion. X-ray diffraction data were collected at Diamond Light Source to a resolution of 2.05 Å. The crystals belonged to space group P21, with eight polypeptide chains in the asymmetric unit arranged as an unusual octamer composed of four domain-swapped IBD dimers. IBD exists as a mixture of monomers and dimers in concentrated solutions, but the dimers are unlikely to be biologically relevant.	Mar 2018

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