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Updated: Jun 7, 2026
Mycobacterium tuberculosis Extracellular Vesicle Enrichment through Size Exclusion Chromatography
Published on: May 19, 2022
Cloning, expression, purification, crystallization and preliminary crystallographic analysis of Rv1698, an outer
Liu Chen1, Demeng Sun, Minhao Wu
1National Laboratory for Physical Science at Microscale, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Abstract:
Rv1698 has been reported to be an important outer membrane channel protein of Mycobacterium tuberculosis with unknown function. Recombinant Rv1698 overexpressed in Escherichia coli was purified in detergent solution and crystallized at 295 K using the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant. The crystals of Rv1698 diffracted to 2.5 Å resolution and belonged to the orthorhombic space group P422, with unit-cell parameters a = b = 122.0, c = 88.9 Å.
