Overexpression, purification, crystallization and data collection ofSulfolobus solfataricusSso6206, a novel highly conserved protein
| Autor: | Malcolm F. White, Lester G. Carter, James H. Naismith, Andrew R. McEwan, Mark Dorward, Muse Oke, Helen Powers, Huanting Liu, Stephen A. McMahon |
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| Rok vydání: | 2006 |
| Předmět: |
Archaeal Proteins
Molecular Sequence Data Size-exclusion chromatography ved/biology.organism_classification_rank.species Biophysics Sequence alignment Biology Crystallography X-Ray medicine.disease_cause Biochemistry Oligomer law.invention chemistry.chemical_compound Structural Biology law Escherichia coli Genetics medicine Molecular replacement Amino Acid Sequence Cloning Molecular Crystallization Protein Structure Quaternary Peptide sequence Sso6206 ved/biology Sulfolobus solfataricus Condensed Matter Physics Crystallography chemistry Crystallization Communications Sequence Alignment |
| Zdroj: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309106003654 |
| Popis: | The novel protein Sso6206 has been crystallized; interestingly, the protein may form large multi-subunit oligomers. Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been overexpressed, purified and crystallized. The protein crystallizes in space group P61/522, with unit-cell parameters a = b = 157.8, c = 307.3 Å. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 Å resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of >9 subunits. |
| Databáze: | OpenAIRE |
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