دورية أكاديمية
أعرض في EDS

High-Resolution Electron Diffraction of Hydrated Protein Crystals at Room Temperature.

التفاصيل البيبلوغرافية
العنوان: High-Resolution Electron Diffraction of Hydrated Protein Crystals at Room Temperature.
المؤلفون: Plana-Ruiz S; NanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.; Servei de Recursos Científics i Tècnics, Universitat Rovira i Virgili, Tarragona 43007, Catalonia, Spain., Gómez-Pérez A; NanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium., Budayova-Spano M; Université Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France., Foley DL; Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland 21218, United States., Portillo-Serra J; NanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium., Rauch E; SIMAP, Grenoble INP, Université Grenoble Alpes, CNRS, F-38000 Grenoble, France., Grivas E; NanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium., Housset D; Université Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France., Das PP; NanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium., Taheri ML; Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland 21218, United States., Nicolopoulos S; NanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium., Ling WL; Université Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.
المصدر: ACS nano [ACS Nano] 2023 Dec 26; Vol. 17 (24), pp. 24802-24813. Date of Electronic Publication: 2023 Oct 27.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101313589 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1936-086X (Electronic) Linking ISSN: 19360851 NLM ISO Abbreviation: ACS Nano Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington D.C. : American Chemical Society
مواضيع طبية MeSH: Electrons* , Proteins*/chemistry, Temperature ; Crystallography, X-Ray ; X-Ray Diffraction
مستخلص: Structural characterization is crucial to understanding protein function. Compared with X-ray diffraction methods, electron crystallography can be performed on nanometer-sized crystals and can provide additional information from the resulting Coulomb potential map. Whereas electron crystallography has successfully resolved three-dimensional structures of vitrified protein crystals, its widespread use as a structural biology tool has been limited. One main reason is the fragility of such crystals. Protein crystals can be easily damaged by mechanical stress, change in temperature, or buffer conditions as well as by electron irradiation. This work demonstrates a methodology to preserve these nanocrystals in their natural environment at room temperature for electron diffraction experiments as an alternative to existing cryogenic techniques. Lysozyme crystals in their crystallization solution are hermetically sealed via graphene-coated grids, and their radiation damage is minimized by employing a low-dose data collection strategy in combination with a hybrid-pixel direct electron detector. Diffraction patterns with reflections of up to 3 Å are obtained and successfully indexed using a template-matching algorithm. These results demonstrate the feasibility of in situ protein electron diffraction. The method described will also be applicable to structural studies of hydrated nanocrystals important in many research and technological developments.
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فهرسة مساهمة: Keywords: electron diffraction; graphene liquid cell; liquid phase electron microscopy; lysozyme; protein electron crystallography
المشرفين على المادة: 0 (Proteins)
تواريخ الأحداث: Date Created: 20231027 Date Completed: 20231227 Latest Revision: 20240829
رمز التحديث: 20240830
مُعرف محوري في PubMed: PMC10753879
DOI: 10.1021/acsnano.3c05378
PMID: 37890869
قاعدة البيانات: MEDLINE
الوصف
تدمد:1936-086X
DOI:10.1021/acsnano.3c05378