Cloning, purification, crystallization and preliminary crystallographic analysis of SecA fromEnterococcus faecalis
| Autor: | Sevil Weinkauf, Markus Fischer, Johannes Scheuring, Winfried Meining |
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| Rok vydání: | 2006 |
| Předmět: |
Proteases
Lysine Biophysics medicine.disease_cause environment and public health Biochemistry Enterococcus faecalis law.invention Bacterial Proteins X-Ray Diffraction Structural Biology law Genetics medicine Asparagine Cloning Molecular Crystallization Escherichia coli Adenosine Triphosphatases Cloning chemistry.chemical_classification SecA Proteins biology Membrane Transport Proteins Condensed Matter Physics biology.organism_classification Amino acid Crystallography Amino Acid Substitution chemistry Crystallization Communications Solvents bacteria SEC Translocation Channels |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:583-585 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309106017544 |
| Popis: | The gene coding for SecA from Enterococcus faecalis was cloned and overexpressed in Escherichia coli. In this protein, the lysine at position 6 was replaced by an asparagine in order to reduce sensitivity towards proteases. The modified protein was purified and crystallized. Crystals diffracting to 2.4 A resolution were obtained using the vapour-diffusion technique. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 A, alpha = gamma = 90.0, beta = 119.1 degrees. A selenomethionine derivative was prepared and is currently being tested in crystallization trials. |
| Databáze: | OpenAIRE |
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