pISSN 2288-6982
eISSN 2288-7105




BioDesign 2023; 11(4): 70-73

Published online December 30, 2023

© Korean Society for Structural Biology

Crystallization and X-ray crystallographic analysis of the extracytoplasmic domain of the sensor histidine kinase CssS from Bacillus subtilis

Pawan Dahal1, Deepak Pathak1 and Eunju Kwon2,3,*

1College of Pharmacy, Yeungnam University, Gyeongsan 38541, Republic of Korea
2Division of Life Science, Gyeongsang National University, Jinju 52828, Republic of Korea
3Research Institute of Molecular Alchemy, Gyeongsang National University, Jinju 52828, Republic of Korea

Correspondence to: *

Received: November 6, 2023; Revised: November 22, 2023; Accepted: November 23, 2023


Bacteria regulate stress-response transcription using two-component systems to adapt to environmental changes. In Bacillus subtilis, the Css two-component system is responsible for counteracting envelope stress caused by heat, protein misfolding, and peptidoglycan stress. This envelope stress is directly recognized by the extracytoplasmic domain of CssS (CssS-ECD). As preliminary studies to understand the stress-sensing mechanism of CssS, CssS-ECD was expressed, purified, and crystallized. Diffraction data of CssS-ECD were collected at a sub-atomic resolution of 0.92 Å. The crystal belongs to the primitive P1 space group with unit cell parameters of a = 27.2, b = 33.7, c = 33.8 (Å), α = 97.7, β = 109.5, and γ = 104.6 (°). The Matthews coefficient of this crystal is calculated to be 1.75 Å3/Da and the corresponding solvent content is 29.6%, assuming that one CssS-ECD is in the crystallographic asymmetric unit.