Related Experiment Video
Updated: Jul 18, 2026
Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Protein preparation, crystallization and preliminary X-ray crystallographic studies of Smu.1392c from Streptococcus
Zeng-Qiang Gao1, Hai-Feng Hou, Yu-He Liang
1Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Beijing, 100049, China.
Abstract:
Smu.1392c is a protein with 158 residues of uncharacterized function. Bioinformatics studies predict it is a putative acetyltransferase. In order to identify its exact function via structural studies, Smu.1392c gene was amplified from Streptococcus mutans genomic DNA and cloned into expression vector PET28a. Smu.1392c was crystallized and diffracted to a resolution of 3 A in-house. The crystal belongs to R32 space group, with unit cell parameters a=b=229.10, c=63.49 A. There are 2 or 3 molecules in the asymmetric unit.
Insights
Researchers characterized the Streptococcus mutans Smu.1392c protein, a putative acetyltransferase. Structural studies were initiated to determine its function, yielding initial crystallographic data.
Area of Science:
- Biochemistry
- Structural Biology
- Microbiology
Background:
- Smu.1392c is a protein from Streptococcus mutans with 158 residues.
- Its function is uncharacterized, though bioinformatics predict it is a putative acetyltransferase.
Purpose of the Study:
- To elucidate the function of Smu.1392c through structural studies.
- To obtain structural data for the Smu.1392c protein.
Main Methods:
- Gene amplification of Smu.1392c from Streptococcus mutans genomic DNA.
- Cloning into the PET28a expression vector.
- Protein crystallization and X-ray diffraction analysis.
Main Results:
- Smu.1392c was successfully crystallized.
- Diffraction data was collected to a resolution of 3 Å.
- The crystal belongs to the R32 space group with specific unit cell parameters (a=b=229.10 Å, c=63.49 Å).
- The asymmetric unit contains 2 or 3 molecules.
Conclusions:
- Initial structural data for Smu.1392c has been obtained.
- This provides a foundation for further structural and functional characterization of this putative acetyltransferase.
More Related Videos
09:31PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
Published on: September 26, 2020
09:55From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016