Abstract
Seven Gd complexes were used in the preparation of heavy-atom derivatives for solving the structure of choline-binding protein F (CbpF), a 36 kDa surface protein from Streptococcus pneumoniae, by the SAD method. CbpF was used as a model system to analyse the phasing capability of each of the derivatives. Three different aspects have been systematically characterized: the efficacy of cocrystallization versus soaking in the binding of the different Gd complexes, their mode of interaction and a comparative study of SAD phasing using synchrotron radiation and using a rotating-anode generator. This study reveals the striking potential of these complexes for SAD phasing using a laboratory source and further reinforces their relevance for high-throughput macromolecular crystallography.
| Original language | English |
|---|---|
| Journal | Acta crystallographica. Section D, Biological crystallography |
| Volume | 65 |
| Issue number | Pt 8 |
| Pages (from-to) | 823-31 |
| Number of pages | 9 |
| ISSN | 2059-7983 |
| DOIs | |
| Publication status | Published - Aug 2009 |
Keywords
- Bacterial Proteins/chemistry
- Carrier Proteins/chemistry
- Choline/metabolism
- Crystallization
- Gadolinium/chemistry
- Macromolecular Substances/chemistry
- Protein Binding
- Protein Conformation
- Streptococcus pneumoniae
- Sulfur/chemistry
- Synchrotrons
- X-Ray Diffraction