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Updated: May 13, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Crystallization and preliminary X-ray crystallographic studies of DnaJ from Streptococcus pneumoniae
Shasha Zhao1, Li Jin, Siqiang Niu
1Key Laboratory of Molecular Biology on Infectious Disease, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, People's Republic of China.
Abstract:
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 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 VM value of 3.24 Å3 Da(-1) and a solvent content of 62.1%.
Insights
This study reports the expression, purification, and preliminary crystallographic analysis of Streptococcus pneumoniae DnaJ (SpDnaJ), a protein involved in bacterial infection and vaccine development.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- DnaJ proteins are molecular chaperones essential for protein folding, complex dissociation, and membrane translocation.
- DnaJ from Streptococcus pneumoniae (SpDnaJ) plays a role in bacterial infections and is a target for vaccine development.
Purpose of the Study:
- To report the expression, purification, crystallization, and preliminary crystallographic analysis of SpDnaJ.
- To provide structural insights into SpDnaJ for potential therapeutic applications.
Main Methods:
- Bacterial expression and purification of SpDnaJ.
- Crystallization of SpDnaJ.
- Preliminary X-ray diffraction analysis.
Main Results:
- SpDnaJ was successfully expressed and purified.
- Crystals of SpDnaJ were obtained, belonging to space groups I222 or I2₁2₁2₁.
- Diffraction data were collected to a resolution of 3.0 Å, with unit-cell parameters a=47.68, b=104.45, c=234.57 Å.
Conclusions:
- The preliminary crystallographic data provide a foundation for future structure determination of SpDnaJ.
- Understanding the structure of SpDnaJ can aid in the development of novel vaccines against Streptococcus pneumoniae infections.
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