Purification, crystallization and preliminary X-ray diffraction studies of the arsenic repressor ArsR from Corynebacterium glutamicum

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 12; pp. 1616 - 1618
• Main Authors: Santha, Sangilimadan, Pandaranayaka, Eswari P. J., Rosen, Barry P., Thiyagarajan, Saravanamuthu
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-12-2011
• Subjects: Arsenic; arsenic repressors; ArsR; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Corynebacterium glutamicum; Corynebacterium glutamicum - chemistry; Crystallization; Crystallization Communications; Crystallography, X-Ray; Derivatives; Diffraction; Proteins; Purification; Trans-Activators - chemistry; Trans-Activators - isolation & purification; X-rays
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309111038966

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.