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.
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.
Monferrer
Dominique
D
IBMB-CSIC, Baldiri Reixach 15, 08028 Barcelona, Spain.
Tralau
Tewes
T
Kertesz
Michael A
MA
Panjikar
Santosh
S
Usón
Isabel
I
D001426:Bacterial Proteins / Q000737:chemistry*; D020604:Comamonas testosteroni / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D014157:Transcription Factors / Q000737:chemistry*
D001426:Bacterial Proteins; D014157:Transcription Factors; C104111:TsaR protein, Comamonas testosteroni