Crystallization and Preliminary X-ray Diffraction Analysis of ScrY, a Specific Bacterial Outer Membrane Porin
| Autor: | Katrin Schülein, Thomas Wacker, Doris Forst, Wolfram Welte, Kay Diederichs, Roland Benz, Werner Kreutz |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Salmonella typhimurium
porin crystallization Porins Trimer chemistry.chemical_compound Bacterial Proteins X-Ray Diffraction Structural Biology ddc:570 membrane protein Sodium dodecyl sulfate Molecular Biology Molecular mass Chemistry Escherichia coli Proteins E. coli Sucrose transport Crystallography Porin Cell envelope Crystallization Bacterial outer membrane Ethylene glycol sucrose transport Bacterial Outer Membrane Proteins |
| Zdroj: | Journal of Molecular Biology. 229:258-262 |
| ISSN: | 0022-2836 |
| DOI: | 10.1006/jmbi.1993.1028 |
| Popis: | The sucrose-specific outer membrane porin ScrY of Salmonella typhimurium was isolated from Escherichia coli K-12 strain KS 26 containing the plasmid pPSO112. The protein was purified to homogeneity by differential extraction of the cell envelope in the presence of the detergents sodium dodecyl sulfate and lauryl (dimethyl)-amine oxide (LDAO). The porin had apparent molecular weights of 58 kDa and 120 kDa for the monomer and for the trimer, respectively, on SDS/PAGE. The purified trimers were crystallized using poly(ethylene glycol) 2000 and the detergents octylglucoside (OG) and hexyl-(dimethyl)-amine oxide (C6DAO). X-ray diffraction of the crystals showed reflections to 2.3 A. The space group of the crystals was R3 and the lattice constants of the hexagonal axes were a = b = 112.85 A and c = 149.9 A. The crystal volume per unit of protein molecular weight was 3.47 A3/Da. |
| Databáze: | OpenAIRE |
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