ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2014
7 Å resolution in protein two-dimensional-crystal X-ray diffraction at Linac Coherent Light Source.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 34 citations in OpenAlex.
- From Oncogenic Signaling Pathways to Single-Cell Sequencing of Immune Cells: Changing the Landscape of Cancer Immunotherapy.Molecules (Basel, Switzerland) · 2021Review
- A fixed-target platform for serial femtosecond crystallography in a hydrated environment.IUCrJ · 2020Article
- Macromolecular Nanocrystal Structural Analysis with Electron and X-Rays: A Comparative Review.Molecules (Basel, Switzerland) · 2019Review
- Nylon mesh-based sample holder for fixed-target serial femtosecond crystallography.Scientific reports · 2019Article
- Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019Review
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- Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene.Nature communications · 2018Article
- Article
- Perspective: Opportunities for ultrafast science at SwissFEL.Structural dynamics (Melville, N.Y.) · 2017Article
- Serial femtosecond crystallography: A revolution in structural biology.Archives of biochemistry and biophysics · 2016Review
- Ultrafast isomerization initiated by X-ray core ionization.Nature communications · 2015Article
- Time-resolved structural studies with serial crystallography: A new light on retinal proteins.Structural dynamics (Melville, N.Y.) · 2015Article
- Possibilities for serial femtosecond crystallography sample delivery at future light sources.Structural dynamics (Melville, N.Y.) · 2015Article
- The birth of a new field.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Article
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25 authors at 7 institutions in 3 countries.
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Abstract
Membrane proteins arranged as two-dimensional crystals in the lipid environment provide close-to-physiological structural information, which is essential for understanding the molecular mechanisms of protein function. Previously, X-ray diffraction from individual two-dimensional crystals did not represent a suitable investigational tool because of radiation damage. The recent availability of ultrashort pulses from X-ray free-electron lasers (XFELs) has now provided a means to outrun the damage. Here, we report on measurements performed at the Linac Coherent Light Source XFEL on bacteriorhodopsin two-dimensional crystals mounted on a solid support and kept at room temperature. By merging data from about a dozen single crystal diffraction images, we unambiguously identified the diffraction peaks to a resolution of 7 Å, thus improving the observable resolution with respect to that achievable from a single pattern alone. This indicates that a larger dataset will allow for reliable quantification of peak intensities, and in turn a corresponding increase in the resolution. The presented results pave the way for further XFEL studies on two-dimensional crystals, which may include pump-probe experiments at subpicosecond time resolution.
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