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Updated: Feb 12, 2026

Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
Published on: April 11, 2021
Purification, crystallization and preliminary X-ray diffraction studies of the arsenic repressor ArsR from
Sangilimadan Santha1, Eswari P J Pandaranayaka, Barry P Rosen
1Center of Excellence in Bioinformatics, School of Biotechnology, Madurai Kamaraj University, Palkalai Nagar, Madurai, Tamilnadu, India.
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.
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