Crystallization and preliminary X‐ray crystallographic studies of DnaJ from Streptococcus pneumoniae. Issue 3 (24th March 2013)

• Record Type: Journal Article
• Authors: Zhao, Shasha; Jin, Li; Niu, Siqiang; Yang, Wei; Zhang, Shaocheng; Guo, Zhen; Zhang, Hongpeng; Huang, Ailong; Yin, Yibing; Wang, Deqiang
• Is Part Of: Acta crystallographica. Volume 69:Issue 3(2013:Mar.)
• Page Start: 267
• Page End: 269
• Publication Date: 2013-03-24
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113001668
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>DnaJ, cooperating with DnaK and GrpE, promotes the folding of unfolded hydrophobic polypeptides, dissociates protein complexes and translocates protein across membranes. Additionally, DnaJ from <italic>Streptococcus pneumoniae</italic> (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 <italic>I</italic>222 or <italic>I</italic>2₁2₁2₁ and the diffraction resolution is 3.0 Å with unit‐cell parameters <italic>a</italic> = 47.68, <italic>b</italic> = 104.45, <italic>c</italic> = 234.57 Å. The crystal most likely contains one molecule in the asymmetric unit, with a <italic>V</italic>_M value of 3.24 ų Da⁻¹ and a solvent content of 62.1%.</p> </abstract>