Open AccessCrystallization and preliminary X‐ray crystallographic studies of DnaJ from Streptococcus pneumoniae
Author(s) -
Zhao Shasha,
Jin Li,
Niu Siqiang,
Yang Wei,
Zhang Shaocheng,
Guo Zhen,
Zhang Hongpeng,
Huang Ailong,
Yin Yibing,
Wang Deqiang
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113001668
Subject(s) - crystallization , crystallography , streptococcus pneumoniae , molecule , protein folding , resolution (logic) , crystal (programming language) , chemistry , space group , x ray crystallography , diffraction , biology , bacteria , biochemistry , physics , genetics , artificial intelligence , computer science , programming language , organic chemistry , optics
DnaJ, cooperating with DnaK and GrpE, promotes the folding of unfolded hydrophobic polypeptides, dissociates protein complexes and translocates protein across membranes. Additionally, DnaJ from Streptococcus pneumoniae (SpDnaJ) is involved in the infectious disease process and is being developed as a potential vaccine to prevent bacterial infection. Here the expression, purification, crystallization and preliminary crystallographic analysis of SpDnaJ are reported. The crystals belong to space groups I 222 or I 2 1 2 1 2 1 and the diffraction resolution is 3.0 Å with unit‐cell parameters a = 47.68, b = 104.45, c = 234.57 Å. The crystal most likely contains one molecule in the asymmetric unit, with a V M value of 3.24 Å 3 Da −1 and a solvent content of 62.1%.