ArticleJournal of applied crystallography2017
Reconstructing three-dimensional protein crystal intensities from sparse unoriented two-axis X-ray diffraction patterns.
Article in Journal of applied crystallography, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.Acta crystallographica. Section D, Structural biology · 2023Article
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- Erratum: Reconstructing three-dimensional protein crystal intensities from sparse unoriented two-axis X-ray diffraction patterns. Corrigendum.Journal of applied crystallography · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
Abstract
Recently, there has been a growing interest in adapting serial microcrystallography (SMX) experiments to existing storage ring (SR) sources. For very small crystals, however, radiation damage occurs before sufficient numbers of photons are diffracted to determine the orientation of the crystal. The challenge is to merge data from a large number of such 'sparse' frames in order to measure the full reciprocal space intensity. To simulate sparse frames, a dataset was collected from a large lysozyme crystal illuminated by a dim X-ray source. The crystal was continuously rotated about two orthogonal axes to sample a subset of the rotation space. With the EMC algorithm [expand-maximize-compress; Loh & Elser (2009).
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