Open AccessCrystallization and preliminary X‐ray analysis of a putative sensor histidine kinase domain: the C‐terminal domain of HksP4 from Aquifex aeolicus VF5
Author(s) -
Horita Shoichiro,
Yamanaka Yosuke,
Yamamura Akihiro,
Okada Akitoshi,
Nakayama Jiro,
Nagata Koji,
Tanokura Masaru
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111018434
Subject(s) - crystallography , crystallization , histidine , adenosine triphosphate , aquifex aeolicus , molecule , chemistry , materials science , stereochemistry , enzyme , escherichia coli , biochemistry , organic chemistry , gene
The histidine kinase domain of the cytoplasmic protein HksP4 from the hyperthermophilic bacterium Aquifex aeolicus VF5, located in the C‐terminal half of the protein, was expressed, purified and crystallized. Diffraction‐quality crystals were obtained in the presence of adenosine triphosphate (ATP) or adenosine 5′‐(β,γ‐imido)triphosphate (AMPPNP) by the sitting‐drop vapour‐diffusion method using PEG 3350 as the precipitant. The crystals obtained in the presence of ATP and AMPPNP diffracted X‐rays to 3.1 and 2.9 Å resolution, respectively, on BL‐5A at Photon Factory (Ibaraki, Japan) and were found to belong to the same space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 80.2, b = 105.5, c = 122.0 Å and a = 81.5, b = 105.5, c = 130.9 Å, respectively. Their Matthews coefficients ( V M = 2.74 and 2.51 Å 3 Da −1 , respectively) indicated that both crystals contained four protein molecules per asymmetric unit.