ArticleIUCrJ2016
Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal.
Article in IUCrJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Accurate atomic resolution XFEL structures of a metalloenzyme reveal key insights into its catalytic mechanism.Nature communications · 2026Article
- Coupled on-line in crystallo UV-Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature.Acta crystallographica. Section D, Structural biology · 2026Article
- Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis.Current opinion in structural biology · 2021Review
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Homogeneous batch micro-crystallization of proteins from ammonium sulfate.Acta crystallographica. Section D, Structural biology · 2021Article
- An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.Science advances · 2021Article
- Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis.Chemical science · 2020Article
- Active Intermediates in Copper Nitrite Reductase Reactions Probed by a Cryotrapping-Electron Paramagnetic Resonance Approach.Angewandte Chemie (International ed. in English) · 2020Article
- High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Data-driven challenges and opportunities in crystallography.Emerging topics in life sciences · 2019Article
- Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.ACS catalysis · 2019Article
- Article
- Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins.IUCrJ · 2019Article
- Synchrotron science in the UK: NINA, the SRS and Diamond.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019Article
- Review
- Titration of ionizable groups in proteins using multiple neutron data sets from a single crystal: application to the small GTPase Ras.Acta crystallographica. Section F, Structural biology communications · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Relating individual protein crystal structures to an enzyme mechanism remains a major and challenging goal for structural biology. Serial crystallography using multiple crystals has recently been reported in both synchrotron-radiation and X-ray free-electron laser experiments. In this work, serial crystallography was used to obtain multiple structures serially from one crystal (MSOX) to study in crystallo enzyme catalysis. Rapid, shutterless X-ray detector technology on a synchrotron MX beamline was exploited to perform low-dose serial crystallography on a single copper nitrite reductase crystal, which survived long enough for 45 consecutive 100 K X-ray structures to be collected at 1.07-1.62 Å resolution, all sampled from the same crystal volume. This serial crystallography approach revealed the gradual conversion of the substrate bound at the catalytic type 2 Cu centre from nitrite to nitric oxide, following reduction of the type 1 Cu electron-transfer centre by X-ray-generated solvated electrons. Significant, well defined structural rearrangements in the active site are evident in the series as the enzyme moves through its catalytic cycle, namely nitrite reduction, which is a vital step in the global denitrification process. It is proposed that such a serial crystallography approach is widely applicable for studying any redox or electron-driven enzyme reactions from a single protein crystal. It can provide a 'catalytic reaction movie' highlighting the structural changes that occur during enzyme catalysis. The anticipated developments in the automation of data analysis and modelling are likely to allow seamless and near-real-time analysis of such data on-site at some of the powerful synchrotron crystallographic beamlines.
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