title: Purification, crystallization and preliminary X-ray diffraction studies of the arsenic repressor ArsR from Corynebacterium glutamicum.
abstract: ArsR is a member of the SmtB/ArsR family of metalloregulatory proteins that regulate prokaryotic arsenic-resistance operons. Here, the crystallization and preliminary X-ray diffraction studies of a cysteine-free derivative of ArsR from Corynebacterium glutamicum (CgArsR-C15/16/55S) are reported. CgArsR-C15/16/55S was expressed, purified, crystallized and X-ray diffraction data were collected to 1.86 Å resolution. The protein crystallized in a tetragonal space group (P4), with unit-cell parameters a = b = 41.84, c = 99.47 Å.
authors.affiliation: Center of Excellence in Bioinformatics, School of Biotechnology, Madurai Kamaraj University, Palkalai Nagar, Madurai, Tamilnadu, India.
authors.forename: Sangilimadan
authors.initials: S
authors.lastname: Santha
authors.forename: Eswari P J
authors.initials: EP
authors.lastname: Pandaranayaka
authors.forename: Barry P
authors.initials: BP
authors.lastname: Rosen
authors.forename: Saravanamuthu
authors.initials: S
authors.lastname: Thiyagarajan
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D048230:Corynebacterium glutamicum / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015534:Trans-Activators / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D001426:Bacterial Proteins; D015534:Trans-Activators