دورية أكاديمية
أعرض في EDS

Rapid screening of in cellulo grown protein crystals via a small-angle X-ray scattering/X-ray powder diffraction synergistic approach.

التفاصيل البيبلوغرافية
العنوان: Rapid screening of in cellulo grown protein crystals via a small-angle X-ray scattering/X-ray powder diffraction synergistic approach.
المؤلفون: Lahey-Rudolph JM; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, Lübeck 23562, Germany.; Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, Hamburg 22607, Germany., Schönherr R; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, Lübeck 23562, Germany.; Photon Science, Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, Hamburg 22607, Germany., Jeffries CM; European Molecular Biology Laboratory (EMBL), Hamburg Outstation, c/o DESY, Notkestrasse 85, Hamburg 22607, Germany., Blanchet CE; European Molecular Biology Laboratory (EMBL), Hamburg Outstation, c/o DESY, Notkestrasse 85, Hamburg 22607, Germany., Boger J; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, Lübeck 23562, Germany., Ferreira Ramos AS; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, Lübeck 23562, Germany., Riekehr WM; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, Lübeck 23562, Germany., Triandafillidis DP; Department of Biology, Section of Genetics, Cell Biology and Development, University of Patras, Patras GR-26500, Greece., Valmas A; Department of Biology, Section of Genetics, Cell Biology and Development, University of Patras, Patras GR-26500, Greece., Margiolaki I; Department of Biology, Section of Genetics, Cell Biology and Development, University of Patras, Patras GR-26500, Greece., Svergun D; European Molecular Biology Laboratory (EMBL), Hamburg Outstation, c/o DESY, Notkestrasse 85, Hamburg 22607, Germany., Redecke L; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, Lübeck 23562, Germany.; Photon Science, Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, Hamburg 22607, Germany.
المصدر: Journal of applied crystallography [J Appl Crystallogr] 2020 Sep 25; Vol. 53 (Pt 5), pp. 1169-1180. Date of Electronic Publication: 2020 Sep 25 (Print Publication: 2020).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley Online Library Country of Publication: United States NLM ID: 9876190 Publication Model: eCollection Cited Medium: Print ISSN: 0021-8898 (Print) Linking ISSN: 00218898 NLM ISO Abbreviation: J Appl Crystallogr Subsets: PubMed not MEDLINE
أسماء مطبوعة: Publication: [Malden, MA] : Wiley Online Library
Original Publication: Copenhagen, Munksgaard International Booksellers and Publishers.
مستخلص: Crystallization of recombinant proteins in living cells is an exciting new approach for structural biology that provides an alternative to the time-consuming optimization of protein purification and extensive crystal screening steps. Exploiting the potential of this approach requires a more detailed understanding of the cellular processes involved and versatile screening strategies for crystals in a cell culture. Particularly if the target protein forms crystalline structures of unknown morphology only in a small fraction of cells, their detection by applying standard visualization techniques can be time consuming and difficult owing to the environmental challenges imposed by the living cells. In this study, a high-brilliance and low-background bioSAXS beamline is employed for rapid and sensitive detection of protein microcrystals grown within insect cells. On the basis of the presence of Bragg peaks in the recorded small-angle X-ray scattering profiles, it is possible to assess within seconds whether a cell culture contains microcrystals, even in a small percentage of cells. Since such information cannot be obtained by other established detection methods in this time frame, this screening approach has the potential to overcome one of the bottlenecks of intracellular crystal detection. Moreover, the association of the Bragg peak positions in the scattering curves with the unit-cell composition of the protein crystals raises the possibility of investigating the impact of environmental conditions on the crystal structure of the intracellular protein crystals. This information provides valuable insights helping to further understand the in cellulo crystallization process.
(© Janine Mia Lahey-Rudolph et al. 2020.)
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فهرسة مساهمة: Keywords: X-ray powder diffraction; in cellulo crystals; protein micro-crystallography; small-angle X-ray scattering
تواريخ الأحداث: Date Created: 20201029 Latest Revision: 20240802
رمز التحديث: 20240802
مُعرف محوري في PubMed: PMC7534541
DOI: 10.1107/S1600576720010687
PMID: 33117106
قاعدة البيانات: MEDLINE
الوصف
تدمد:0021-8898
DOI:10.1107/S1600576720010687