Crystallization and preliminary X-ray crystallographic studies of DnaJ from Streptococcus pneumoniae

被引：1
|
作者：
Zhao, Shasha [1 ]
Jin, Li [2 ]
Niu, Siqiang [2 ]
Yang, Wei [1 ]
Zhang, Shaocheng [1 ]
Guo, Zhen [2 ]
Zhang, Hongpeng [2 ]
Huang, Ailong [1 ]
Yin, Yibing [2 ]
Wang, Deqiang [1 ,2 ]
机构：
[1] Chongqing Med Univ, Key Lab Mol Biol Infect Dis, Chongqing 400016, Peoples R China
[2] Chongqing Med Univ, Dept Lab Med, Chongqing 400016, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
关键词：
DnaJ; Streptococcus pneumoniae; ESCHERICHIA-COLI DNAJ; CONSERVED J-DOMAIN; MOLECULAR REPLACEMENT; ATPASE ACTIVITY; CHAPERONE; TRANSLOCATION; REPLICATION; STIMULATE; HSP70; HSP40;
D O I：
10.1107/S1744309113001668
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 I222 or I212121 and the diffraction resolution is 3.0 angstrom with unit-cell parameters a = 47.68, b = 104.45, c = 234.57 angstrom. The crystal most likely contains one molecule in the asymmetric unit, with a VM value of 3.24 angstrom 3Da1 and a solvent content of 62.1%.
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收藏
页码：267 / 269
页数：3
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