Purification, crystallization and preliminary X-ray analysis of IMP-18, a class B carbapenemase fromPseudomonas aeruginosa
| Autor: | Kazuhiro Tateda, Takamitsu Furuyama, Akiko Shimizu-Ibuka, Nancy D. Hanson, Norimasa Ohya, Yoshikazu Ishii |
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| Rok vydání: | 2013 |
| Předmět: |
Biophysics
Gene Expression Biology Crystallography X-Ray medicine.disease_cause Biochemistry beta-Lactamases law.invention Crystal Hydrolysis Tetragonal crystal system Structural Biology law Escherichia coli polycyclic compounds Genetics medicine Crystallization Pseudomonas aeruginosa Resolution (electron density) biochemical phenomena metabolism and nutrition bacterial infections and mycoses Condensed Matter Physics Recombinant Proteins enzymes and coenzymes (carbohydrates) Crystallography Crystallization Communications Recombinant DNA bacteria |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:1397-1400 |
| ISSN: | 1744-3091 |
| Popis: | Class B β-lactamases are known as metallo-β-lactamases (MBLs) and they hydrolyze most β-lactams, including carbapenems. IMP-18, an MBL cloned from Pseudomonas aeruginosa, was overexpressed, purified and crystallized by vapour diffusion for X-ray crystallographic analysis. Preliminary X-ray analysis showed that the crystal diffracted to 2.4 Å resolution and belonged to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 120.77, c = 96.54 Å, α = β = γ = 90°, suggesting the presence of two molecules in the asymmetric unit. |
| Databáze: | OpenAIRE |
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