Open AccessExpression, purification and X‐ray characterization of residues 18–230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae
Author(s) -
RiboldiTunnicliffe Alan,
Bent Colin J.,
Isaacs Neil W.,
Mitchell Timothy J.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904004573
Subject(s) - streptococcus pneumoniae , monoclinic crystal system , escherichia coli , histidine , resolution (logic) , microbiology and biotechnology , crystallography , chemistry , gene , biology , biochemistry , crystal structure , enzyme , artificial intelligence , computer science , antibiotics
A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18–230) was cloned and overexpressed in Escherichia coli . The purified protein was crystallized using the sitting‐drop vapour‐diffusion technique. Crystals belong to the monoclinic space group C 2, with unit‐cell parameters a = 62.19, b = 35.9, c = 72.54 Å, β = 90.01°. The crystals diffract X‐rays to beyond 1.2 Å resolution.