Cargando…
Determination of crystallographic intensities from sparse data
X-ray serial microcrystallography involves the collection and merging of frames of diffraction data from randomly oriented protein microcrystals. The number of diffracted X-rays in each frame is limited by radiation damage, and this number decreases with crystal size. The data in the frame are said...
Autores principales: | Ayyer, Kartik, Philipp, Hugh T., Tate, Mark W., Wierman, Jennifer L., Elser, Veit, Gruner, Sol M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285878/ https://www.ncbi.nlm.nih.gov/pubmed/25610625 http://dx.doi.org/10.1107/S2052252514022313 |
Ejemplares similares
-
Solving structure with sparse, randomly-oriented x-ray data
por: Philipp, Hugh T., et al.
Publicado: (2012) -
Reconstructing three-dimensional protein crystal intensities from sparse unoriented two-axis X-ray diffraction patterns
por: Lan, Ti-Yen, et al.
Publicado: (2017) -
Protein crystal structure from non-oriented, single-axis sparse X-ray data
por: Wierman, Jennifer L., et al.
Publicado: (2016) -
Reconstructing three-dimensional protein crystal intensities from sparse unoriented two-axis X-ray diffraction patterns. Corrigendum
por: Lan, Ti-Yen, et al.
Publicado: (2018) -
Solving protein structure from sparse serial microcrystal diffraction data at a storage-ring synchrotron source
por: Lan, Ti-Yen, et al.
Publicado: (2018)