As the ternary complex is more flexible in solution, I am wondering whether the conformation of the crystal state of the ternary complex is the same as it in solution.
As far as I know the crystal structure can indeed be and in most cases is a valid representation of the native protein conformation and/or protein complexes. One should however always do additional experiments to either confirm oligomerisation states found in the crystal or the protein-protein interface in the case of complexes.
The successful preparation of a protein crystal is related to the special solution conditions, which cannot truly reflect the real conformation of the protein in vivo and solution. Therefore, it is also necessary to use the NMR analysis as an auxiliary means. In addition, compared with single-crystal X-ray diffraction technology, cryo-electron microscopy technology keeps protein molecules closer to their native state.
https://www.creative-biostructure.com/comparison-of-crystallography-nmr-and-em_6.htm
Roger Davis Thanks for your reply and the web link, they are really useful. So, have you ever read some articles which studies the differences between the crystal structure of protein and its native state ?
- Badges
- Science topic
- Similar topics
- Physical Sciences
- Materials Science
- Materials
- Nanomaterials