Open AccessCloning, expression, purification, crystallization and preliminary X‐ray analysis of the pilus‐associated sortase C from Streptococcus pneumoniae
Author(s) -
Neiers F.,
Madhurantakam C.,
Fälker S.,
Normark S.,
HenriquesNormark B.,
Achour A.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108040025
Subject(s) - pilus , crystallization , streptococcus pneumoniae , sortase , crystal (programming language) , protein subunit , crystallography , cloning (programming) , chemistry , microbiology and biotechnology , biology , bacterial protein , biochemistry , gene , escherichia coli , organic chemistry , computer science , programming language , antibiotics
The pilus‐associated sortase C from Streptococcus pneumoniae (SrtC or Srt‐2) acts as a polymerase for the pilus subunit proteins RrgA and RrgB. Here, the crystallization and preliminary X‐ray diffraction analysis of three crystal forms of SrtC are reported. One crystal form belongs to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 48.9, b = 96.9, c = 98.9 Å, α = β = γ = 90°. The other two crystal forms belong to space group P 222, with unit‐cell parameters a = 48.8, b = 97.2, c = 99.2 Å, α = β = γ = 90° and a = 48.6, b = 96.5, c = 98.8 Å, α = β = γ = 90°, respectively. Preliminary analysis indicates the presence of two molecules in the asymmetric unit of the crystal for all three forms.