title: Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of initiation factor 1 from Mycobacterium tuberculosis.
abstract: 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 P2(1)2(1)2, with two molecules per asymmetric unit which are related by translational symmetry.
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Georgios N
authors.initials: GN
authors.lastname: Hatzopoulos
authors.forename: Jochen
authors.initials: J
authors.lastname: Mueller-Dieckmann
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D008970:Molecular Weight; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000235:genetics; D039861:Prokaryotic Initiation Factor-1 / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification*
chemical_list: D001426:Bacterial Proteins; D039861:Prokaryotic Initiation Factor-1