ArticleStructural dynamics (Melville, N.Y.)2015
Room temperature structures beyond 1.5 Å by serial femtosecond crystallography.
Article in Structural dynamics (Melville, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- The dramatic development of X-ray photocrystallography over the past six decades.Structural dynamics (Melville, N.Y.) · 2017Article
- A short history of structure based research on the photocycle of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2017Review
- Graphene-based microfluidics for serial crystallography.Lab on a chip · 2016Article
- Assessment of microcrystal quality by transmission electron microscopy for efficient serial femtosecond crystallography.Archives of biochemistry and biophysics · 2016Review
- Protein crystal screening and characterization for serial femtosecond nanocrystallography.Scientific reports · 2016Article
- Accurate determination of segmented X-ray detector geometry.Optics express · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
About 2.5 × 10(6) snapshots on microcrystals of photoactive yellow protein (PYP) from a recent serial femtosecond crystallographic (SFX) experiment were reanalyzed to maximum resolution. The resolution is pushed to 1.46 Å, and a PYP structural model is refined at that resolution. The result is compared to other PYP models determined at atomic resolution around 1 Å and better at the synchrotron. By comparing subtleties such as individual isotropic temperature factors and hydrogen bond lengths, we were able to assess the quality of the SFX data at that resolution. We also show that the determination of anisotropic temperature factor ellipsoids starts to become feasible with the SFX data at resolutions better than 1.5 Å.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.