View source for 7swa


==MicroED structure of proteinase K from a 320 nm thick lamella measured at 300 kV==
<StructureSection load='7swa' size='340' side='right'caption='[[7swa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7swa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SWA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7swa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7swa OCA], [https://pdbe.org/7swa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7swa RCSB], [https://www.ebi.ac.uk/pdbsum/7swa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7swa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
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== Publication Abstract from PubMed ==
The relationship between sample thickness and quality of data obtained is investigated by microcrystal electron diffraction (MicroED). Several electron microscopy (EM) grids containing proteinase K microcrystals of similar sizes from the same crystallization batch were prepared. Each grid was transferred into a focused ion beam and a scanning electron microscope in which the crystals were then systematically thinned into lamellae between 95- and 1,650-nm thick. MicroED data were collected at either 120-, 200-, or 300-kV accelerating voltages. Lamellae thicknesses were expressed in multiples of the corresponding inelastic mean free path to allow the results from different acceleration voltages to be compared. The quality of the data and subsequently determined structures were assessed using standard crystallographic measures. Structures were reliably determined with similar quality from crystalline lamellae up to twice the inelastic mean free path. Lower resolution diffraction was observed at three times the mean free path for all three accelerating voltages, but the data quality was insufficient to yield structures. Finally, no coherent diffraction was observed from lamellae thicker than four times the calculated inelastic mean free path. This study benchmarks the ideal specimen thickness with implications for all cryo-EM methods.

Benchmarking the ideal sample thickness in cryo-EM.,Martynowycz MW, Clabbers MTB, Unge J, Hattne J, Gonen T Proc Natl Acad Sci U S A. 2021 Dec 7;118(49):e2108884118. doi: , 10.1073/pnas.2108884118. PMID:34873060<ref>PMID:34873060</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7swa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Parengyodontium album]]
[[Category: Clabbers MTB]]
[[Category: Gonen T]]
[[Category: Hattne J]]
[[Category: Martynowycz MW]]
[[Category: Unge J]]