ArticleIUCrJ2019
Subatomic resolution X-ray structures of green fluorescent protein.
Article in IUCrJ, 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.
- Article
- Macromolecular crystallography at SPring-8 and SACLA.Journal of synchrotron radiation · 2025Article
- Structural characterization of green fluorescent protein in the I-state.Scientific reports · 2024Article
- Impact of the Protein Environment on Two-Photon Absorption Cross-Sections of the GFP Chromophore Anion Resolved at the XMCQDPT2 Level of Theory.International journal of molecular sciences · 2023Article
- Measurement of charges and chemical bonding in a cryo-EM structure.Communications chemistry · 2023Article
- Experimental evidence for the benefits of higher X-ray energies for macromolecular crystallography.IUCrJ · 2021Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- What is the Optimal Size of the Quantum Region in Embedding Calculations of Two-Photon Absorption Spectra of Fluorescent Proteins?Journal of chemical theory and computation · 2020Article
- Mechanism of Color and Photoacidity Tuning for the Protonated Green Fluorescent Protein Chromophore.Journal of the American Chemical Society · 2020Article
- A shared vision for macromolecular crystallography over the next five years.Structural dynamics (Melville, N.Y.) · 2019Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Green fluorescent protein (GFP) is a light-emitting protein that does not require a prosthetic group for its fluorescent activity. As such, GFP has become indispensable as a molecular tool in molecular biology. Nonetheless, there has been no subatomic elucidation of the GFP structure owing to the structural polymorphism around the chromophore. Here, subatomic resolution X-ray structures of GFP without the structural polymorphism are reported. The positions of H atoms, hydrogen-bonding network patterns and accurate geometric parameters were determined for the two protonated forms. Compared with previously determined crystal structures and theoretically optimized structures, the anionic chromophores of the structures represent the authentic resonance state of GFP. In addition, charge-density analysis based on atoms-in-molecules theory and noncovalent interaction analysis highlight weak but substantial interactions between the chromophore and the protein environment. Considered with the derived chemical indicators, the lone pair-π interactions between the chromophore and Thr62 should play a sufficient role in maintaining the electronic state of the chromophore. These results not only reveal the fine structural features that are critical to understanding the properties of GFP, but also highlight the limitations of current quantum-chemical calculations.
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