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Crystallization and preliminary X-ray studies of SdiA fromEscherichia coli
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64:19-21
- Publication Year :
- 2007
- Publisher :
- International Union of Crystallography (IUCr), 2007.
-
Abstract
- SdiA enhances cell division by regulating the ftsQAZ operon in Escherichia coli as a transcription activator. In addition, SdiA is suggested to play a role in detecting quorum signals that emanate from other species. It is therefore a homologue of LuxR, a cognate quorum-sensing receptor that recognizes a quorum signal and activates the quorum responses. To elucidate the role of SdiA and its functional and structural relationship to LuxR, structural studies were performed on E. coli SdiA. Recombinant SdiA was overexpressed, purified and crystallized at 287 K using the hanging-drop vapour-diffusion method. X-ray diffraction data from a native crystal were collected with 99.7% completeness to 2.7 A resolution with an R(merge) of 6.0%. The crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 130.47, c = 125.23 A.
- Subjects :
- genetic structures
Cell division
Operon
Biophysics
Biology
Crystallography, X-Ray
medicine.disease_cause
Biochemistry
law.invention
Plasmid
X-Ray Diffraction
Structural Biology
law
Escherichia coli
Genetics
medicine
Receptor
Escherichia coli Proteins
food and beverages
biochemical phenomena, metabolism, and nutrition
Condensed Matter Physics
Recombinant Proteins
Quorum sensing
Crystallization Communications
Conjugation, Genetic
Trans-Activators
Recombinant DNA
bacteria
Crystallization
Plasmids
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 64
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....6e6e261de3e313526bb060e3ae93d342