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Cloning, expression, purification, crystallization and preliminary X‐ray crystallographic analysis of initiation factor 1 from Mycobacterium tuberculosis
Author(s) -
Hatzopoulos Georgios N.,
MuellerDieckmann Jochen
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910700437x
Subject(s) - cloning (programming) , crystallization , mycobacterium tuberculosis , crystallography , tuberculosis , materials science , microbiology and biotechnology , biology , chemistry , medicine , pathology , organic chemistry , computer science , programming language
Initiation factor 1 (IF‐1; Rv3462c) from Mycobacterium tuberculosis , a component of the 30S initiation complex, was cloned and heterologously expressed in Escherichia coli . The protein was purified by affinity and size‐exclusion chromatography and crystallized. A complete data set has been collected to high resolution. The crystals belonged to space group P 2 1 2 1 2, with two molecules per asymmetric unit which are related by translational symmetry.

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