Abstract
Crystallization conditions are reported for an engineered cephalosporin acylase based on the sequence of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas strain N176. Initial crystals were grown using polyethylene glycol as a crystallizing agent; however, these crystals diffracted poorly and exhibited high mosaicity. A dehydration procedure in which crystals were transferred to a solution containing a higher concentration of polyethylene glycol as well as glycerol improved the diffraction quality such that a 1.57 Å diffraction data set could be obtained.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 808-810 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 66 |
| Issue number | 7 |
| DOIs | |
| State | Published - 2010 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics
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Anandan, A., Vallet, C., Coyle, T., Moustafa, I. M., & Vrielink, A. (2010). Crystallization and preliminary diffraction analysis of an engineered cephalosporin acylase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(7), 808-810. https://doi.org/10.1107/S1744309110017185