Crystallization and preliminary X-ray analysis of a γ-lactamase
| Autor: | Michail N. Isupov, Jennifer A. Littlechild, Irene S. Gonsalvez |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Sequence Homology Amino Acid Resolution (electron density) Betaproteobacteria Synchrotron radiation General Medicine Polyethylene glycol Crystallography X-Ray Mass Spectrometry Amidohydrolases Polyethylene Glycols law.invention Crystallography Hydrolysis chemistry.chemical_compound Enzyme Stereospecificity Biotransformation chemistry Structural Biology law Enzyme Inhibitors Crystallization Sequence Alignment |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 57:284-286 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444900016838 |
| Popis: | An enzyme from Comomonas acidovorans has been isolated that is specific for the stereospecific hydrolysis of (+)gamma-lactam. This so-called (+)gamma-lactamase has important applications in biotransformation reactions. The enzyme has been crystallized by vapour-phase diffusion using polyethylene glycol 4000 as a precipitant. Addition of a detergent, beta-octylglucoside, was found to be essential for obtaining diffraction-quality crystals. The crystals grow in the space group P1, with unit-cell parameters a = 63.0, b = 93.2, c = 152.4 A, alpha = 104.3, beta = 92.6, gamma = 108.5 degrees, and diffract to 2 A resolution using synchrotron radiation. Native data from these crystals have been collected to 2.4 A. |
| Databáze: | OpenAIRE |
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