Electron cryomicroscopy: Difference between revisions
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==Resolution== | ==Resolution== | ||
<StructureSection load='' size='350' side='right' caption='' scene='80/805038/Insulin_receptor/6'> | <StructureSection load='' size='350' side='right' caption='' scene='80/805038/Insulin_receptor/6'> | ||
The median [[resolution]] of cryo-EM structures deposited in '''2020''' in the [[Protein Data Bank]] was 3.5 Å (improved from 3.8 Å in 2018, and 4.2 Å in 2016)<ref name="mvr">See cryo-EM Resolution compared with X-ray diffraction resolution: | The median [[resolution]] of cryo-EM structures deposited in '''2020''' in the [[Protein Data Bank]] was 3.5 Å (improved from 3.8 Å in 2018, and 4.2 Å in 2016)<ref name="mvr">See cryo-EM Resolution compared with X-ray diffraction resolution: | ||
[http://tinyurl.com/method-vs-resolution tinyurl.com/method-vs-resolution].</ref>. For comparison, the median resolution of X-ray crystallographic entries in the PDB has been 2.0 Å for many years<ref name="mvr" />. When resolution improves by a factor of 2, the available data (to support the coordinate model) goes up by a factor of 8. For example, a 2.4 Å resolution structure is a great improvement over a 3.0 Å resolution structure because the number of available measurements doubles. | [http://tinyurl.com/method-vs-resolution tinyurl.com/method-vs-resolution].</ref>. For comparison, the median resolution of X-ray crystallographic entries in the PDB has been 2.0 Å for many years<ref name="mvr" />. When resolution improves by a factor of 2, the available data (to support the coordinate model) goes up by a factor of 8. For example, a 2.4 Å resolution structure is a great improvement over a 3.0 Å resolution structure because the number of available measurements doubles. | ||