title: High crystallizability under air-exclusion conditions of the full-length LysR-type transcriptional regulator TsaR from Comamonas testosteroni T-2 and data-set analysis for a MIRAS structure-solution approach.
abstract: The full-length LysR-type transcriptional regulator TsaR from Comamonas testosteroni T-2 was heterologously overexpressed in Escherichia coli, purified and stabilized under conditions that favoured its rapid crystallization using the microbatch-under-oil technique. The purified protein was highly crystallizable and two different crystal forms were readily obtained. However, only monoclinic crystals gave diffraction beyond 2 A and there was a slight variation in unit-cell parameters between crystals. The only other LysR-type regulator for which a full-length crystal form is available is CbnR, but no solution could be obtained when this was used as a model in molecular replacement. Mercury and xenon derivatives were therefore produced in order to phase the structure using a MIRAS approach.
authors.affiliation: IBMB-CSIC, Baldiri Reixach 15, 08028 Barcelona, Spain.
authors.forename: Dominique
authors.initials: D
authors.lastname: Monferrer
authors.forename: Tewes
authors.initials: T
authors.lastname: Tralau
authors.forename: Michael A
authors.initials: MA
authors.lastname: Kertesz
authors.forename: Santosh
authors.initials: S
authors.lastname: Panjikar
authors.forename: Isabel
authors.initials: I
authors.lastname: Usón
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D020604:Comamonas testosteroni / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D014157:Transcription Factors / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D014157:Transcription Factors; C104111:TsaR protein, Comamonas testosteroni