The most common method in the structure determination of proteins using x-ray crystallography is Molecular Replacement (MR), which relies on structural information from proteins that share sequence similarity with the target protein. However, MR is non-trivial when the sequence similarity is less than 30%, and the selection of a suitable starting model is onerous due to inherent model error. We have developed a method, employing objective pruning of multiply aligned structures, that produces superior candidate models for structure elucidation. This will result in a major new tool to solve the three-dimensional structures of proteins in a significantly shorter timeframe than is currently possible.
|Effective start/end date||2/01/08 → 31/12/10|
- Australian Research Council (ARC): AUD240,000.00
- Australian Research Council (ARC)