Name
Abstract | ||
|---|---|---|
Protein X-ray crystallography, the determination of three-dimensional structures of protein molecules from crystal X-ray diffraction data, requires determining the phases of the diffraction signal, since only the amplitude is measured. This so-called phase problem is a key component of protein X-ray crystallography. Most current methods for phasing are experimentally based and utilise either additional diffraction data from modified crystals or knowledge of the structure of a related protein. Ab initio phasing refers to computational methods that utilise only the measured diffraction amplitudes and some a priori information on protein electron densities, and potentially offer a dramatic reduction in effort over experimental methods. A key question in ab initio phasing is whether the diffraction amplitudes and the a priori information are sufficient to uniquely define the phases. The question of uniqueness is examined here for the case of a priori information on the molecular envelope. |
Year | DOI | Venue |
|---|---|---|
2015 | 10.1109/IVCNZ.2015.7761511 | 2015 International Conference on Image and Vision Computing New Zealand (IVCNZ) |
Keywords | Field | DocType |
ab initio phase retrieval,macromolecular X-ray crystallography,protein X-ray crystallography,3D protein molecule structure,crystal X-ray diffraction data,diffraction signal amplitude,phase problem,ab initio phasing,protein electron density,molecular envelope | Uniqueness,Chemical physics,X-ray crystallography,Phase retrieval,Pattern recognition,Computer science,Phase problem,Crystal,Phaser,Artificial intelligence,Ab initio,Diffraction | Conference |
ISSN | ISBN | Citations |
2151-2191 | 978-1-5090-0358-7 | 0 |
PageRank | References | Authors |
0.34 | 0 | 2 |
Name | Order | Citations | PageRank |
|---|---|---|---|
| Romain D. Arnal | 1 | 0 | 0.68 |
| Rick P. Millane | 2 | 4 | 4.83 |