Related Experiment Video
Updated: Jul 16, 2026
High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of initiation
Georgios N Hatzopoulos1, Jochen Mueller-Dieckmann
1EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
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.
More Related Videos
22:10Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
Published on: June 28, 2013
09:31PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
Published on: September 26, 2020