ArticleThe Journal of biological chemistry2019
Non-cryogenic structure of a chloride pump provides crucial clues to temperature-dependent channel transport efficiency.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Review of serial femtosecond crystallography including the COVID-19 pandemic impact and future outlook.Structure (London, England : 1993) · 2023Review
- Conformational alterations in unidirectional ion transport of a light-driven chloride pump revealed using X-ray free electron lasers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Early-stage dynamics of chloride ion-pumping rhodopsin revealed by a femtosecond X-ray laser.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Molecular mechanism of light-driven sodium pumping.Nature communications · 2020Article
- A fixed-target platform for serial femtosecond crystallography in a hydrated environment.IUCrJ · 2020Article
- The XFEL Protein Crystallography: Developments and Perspectives.International journal of molecular sciences · 2019Article
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Authors and funding
20 authors at 5 institutions in 4 countries.
Funding
Abstract
Non-cryogenic protein structures determined at ambient temperature may disclose significant information about protein activity. Chloride-pumping rhodopsin (ClR) exhibits a trend to hyperactivity induced by a change in the photoreaction rate because of a gradual decrease in temperature. Here, to track the structural changes that explain the differences in CIR activity resulting from these temperature changes, we used serial femtosecond crystallography (SFX) with an X-ray free electron laser (XFEL) to determine the non-cryogenic structure of ClR at a resolution of 1.85 Å, and compared this structure with a cryogenic ClR structure obtained with synchrotron X-ray crystallography. The XFEL-derived ClR structure revealed that the all-
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