Crystallization and preliminary X-ray diffraction studies of the C-terminal domain ofChlamydia trachomatisCdsD
| Autor: | Gitte Meriläinen, Rik K. Wierenga |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Protein family
Biophysics Chlamydia trachomatis Biology medicine.disease_cause Biochemistry Chromatography Affinity Type three secretion system Bacterial Proteins X-Ray Diffraction Structural Biology Genetics medicine Inner membrane Bacterial Secretion Systems Escherichia coli chemistry.chemical_classification C-terminus Resolution (electron density) Condensed Matter Physics Protein Structure Tertiary Amino acid Crystallography chemistry Crystallization Communications biological sciences health occupations bacteria Crystallization |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 70:1431-1433 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x14019712 |
| Popis: | The inner membrane ring of the bacterial type III secretion system (TTSS) is composed of two proteins. InChlamydia trachomatisthis ring is formed by CdsD (gene nameCT_664) and CdsJ (gene nameCTA_0609). CdsD consists of 829 amino acids. The last 400 amino acids at its C-terminal end relate it to the type III secretion system YscD/HrpQ protein family. The C-terminal domain, consisting of amino acids 558–771, ofC. trachomatisCdsD was overexpressed inEscherichia coliand purified using immobilized metal-affinity chromatography (IMAC) and size-exclusion chromatography. The protein was crystallized using the vapour-diffusion method. A data set was collected to 2.26 Å resolution. The crystals have the symmetry of space groupC2, with unit-cell parametersa= 106.60,b= 23.91,c= 118.65 Å, β = 104.95°. According to the data analysis there is expected to be one molecule in the asymmetric unit, with a Matthews coefficient of 3.0 Å3 Da−1. |
| Databáze: | OpenAIRE |
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