6cla: Difference between revisions
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==2.80 A MicroED structure of proteinase K at 6.0 e- / A^2== | |||
<StructureSection load='6cla' size='340' side='right'caption='[[6cla]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6cla]] 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=6CLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CLA 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]] 2.8Å</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=6cla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cla OCA], [https://pdbe.org/6cla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cla RCSB], [https://www.ebi.ac.uk/pdbsum/6cla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cla ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Micro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering with diffraction to allow structure determination from nano-sized crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data. | |||
Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.,Hattne J, Shi D, Glynn C, Zee CT, Gallagher-Jones M, Martynowycz MW, Rodriguez JA, Gonen T Structure. 2018 May 1;26(5):759-766.e4. doi: 10.1016/j.str.2018.03.021. Epub 2018, Apr 26. PMID:29706530<ref>PMID:29706530</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6cla" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Parengyodontium album]] | |||
[[Category: Gallagher-Jones M]] | |||
[[Category: Glynn C]] | |||
[[Category: Gonen T]] | |||
[[Category: Hattne J]] | |||
[[Category: Martynowycz MW]] | |||
[[Category: Rodriguez JA]] | |||
[[Category: Shi D]] | |||
[[Category: Zee C-T]] | |||
Latest revision as of 18:07, 4 October 2023
2.80 A MicroED structure of proteinase K at 6.0 e- / A^22.80 A MicroED structure of proteinase K at 6.0 e- / A^2
Structural highlights
FunctionPRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedMicro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering with diffraction to allow structure determination from nano-sized crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data. Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.,Hattne J, Shi D, Glynn C, Zee CT, Gallagher-Jones M, Martynowycz MW, Rodriguez JA, Gonen T Structure. 2018 May 1;26(5):759-766.e4. doi: 10.1016/j.str.2018.03.021. Epub 2018, Apr 26. PMID:29706530[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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