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TitleMethods for merging data sets in electron cryo-microscopy.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 75, Issue Pt 9, Page 782-791, Year 2019
Publish dateSep 1, 2019
AuthorsMax E Wilkinson / Ananthanarayanan Kumar / Ana Casañal /
PubMed AbstractRecent developments have resulted in electron cryo-microscopy (cryo-EM) becoming a useful tool for the structure determination of biological macromolecules. For samples containing inherent ...Recent developments have resulted in electron cryo-microscopy (cryo-EM) becoming a useful tool for the structure determination of biological macromolecules. For samples containing inherent flexibility, heterogeneity or preferred orientation, the collection of extensive cryo-EM data using several conditions and microscopes is often required. In such a scenario, merging cryo-EM data sets is advantageous because it allows improved three-dimensional reconstructions to be obtained. Since data sets are not always collected with the same pixel size, merging data can be challenging. Here, two methods to combine cryo-EM data are described. Both involve the calculation of a rescaling factor from independent data sets. The effects of errors in the scaling factor on the results of data merging are also estimated. The methods described here provide a guideline for cryo-EM users who wish to combine data sets from the same type of microscope and detector.
External linksActa Crystallogr D Struct Biol / PubMed:31478901 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

EMDB-10140:
Post-catalytic P complex spliceosome at 3.3 angstrom resolution from merging data sets
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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