Open AccessHigh 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
Author(s) -
Monferrer Dominique,
Tralau Tewes,
Kertesz Michael A.,
Panjikar Santosh,
Usón Isabel
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108019738
Subject(s) - comamonas testosteroni , regulator , escherichia coli , monoclinic crystal system , crystallization , chemistry , transcriptional regulation , crystallography , crystal structure , biochemistry , transcription factor , gene , organic chemistry
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 Å 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.