Cargando…
Protein structure determination by electron diffraction using a single three-dimensional nanocrystal
Three-dimensional nanometre-sized crystals of macromolecules currently resist structure elucidation by single-crystal X-ray crystallography. Here, a single nanocrystal with a diffracting volume of only 0.14 µm(3), i.e. no more than 6 × 10(5) unit cells, provided sufficient information to determine t...
Autores principales: | Clabbers, M. T. B., van Genderen, E., Wan, W., Wiegers, E. L., Gruene, T., Abrahams, J. P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5586247/ https://www.ncbi.nlm.nih.gov/pubmed/28876237 http://dx.doi.org/10.1107/S2059798317010348 |
Ejemplares similares
-
Ab initio structure determination of nanocrystals of organic pharmaceutical compounds by electron diffraction at room temperature using a Timepix quantum area direct electron detector
por: van Genderen, E., et al.
Publicado: (2016) -
Ab initio structure determination of nanocrystals of organic pharmaceutical compounds by electron diffraction at room temperature using a Timepix quantum area direct electron detector. Corrigendum
por: van Genderen, E., et al.
Publicado: (2018) -
Electron diffraction data processing with DIALS
por: Clabbers, Max T. B., et al.
Publicado: (2018) -
Reducing dynamical electron scattering reveals hydrogen atoms
por: Clabbers, Max T. B., et al.
Publicado: (2019) -
Lattice filter for processing image data of three-dimensional protein nanocrystals
por: van Genderen, E., et al.
Publicado: (2016)