Open AccessCloning, expression, purification, crystallization and preliminary X‐ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis
Author(s) -
Patra Dhabaleswar,
Srikalaivani R.,
Misra Ashish,
Singh D. D.,
Selvaraj M.,
Vijayan M.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110042892
Subject(s) - lectin , crystallization , cloning (programming) , mycobacterium tuberculosis , concanavalin a , c type lectin , biology , molecular cloning , biochemistry , chemistry , microbiology and biotechnology , peptide sequence , tuberculosis , gene , in vitro , medicine , organic chemistry , pathology , computer science , programming language
A secreted lectin, Rv1419, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized and the crystals have been characterized. This represents the first X‐ray investigation of a lectin or lectin‐like molecule from the pathogen. The cubic crystals contain one molecule in the asymmetric unit. Sequence comparisons indicate that the lectin has a β‐trefoil fold and belongs to a well characterized family of carbohydrate‐binding modules. Structural analysis of the crystals is in progress.