Open AccessCrystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response‐regulator homologue from Streptococcus pneumoniae
Author(s) -
RiboldiTunnicliffe Alan,
Trombe MarieClaude,
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/s0907444904005712
Subject(s) - mica , streptococcus pneumoniae , crystallography , mutant , regulator , crystallization , effector , resolution (logic) , chemistry , materials science , biology , gene , genetics , biochemistry , bacteria , organic chemistry , artificial intelligence , computer science , composite material
RR02 (MicA) is an essential bacterial protein that belongs to the YycF family of response regulators and consists of two domains: an N‐terminal receiver domain and a C‐terminal effector domain. Streptococcus pneumoniae RR02 (MicA; residues 2–234) has been crystallized using the sitting‐drop vapour‐diffusion technique. The crystals belong to space group P 2 1 , with unit‐cell parameters a = 46.46, b = 32.61, c = 63.35 Å, β = 90.01°. X‐ray diffraction data have been collected to 1.93 Å resolution.