6cla: Difference between revisions

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-'''Unreleased structure'''
-The entry 6cla is ON HOLD  until Paper Publication
+==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]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cla]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CLA FirstGlance]. <br>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cla OCA], [http://pdbe.org/6cla PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cla RCSB], [http://www.ebi.ac.uk/pdbsum/6cla PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cla ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6cla" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Parengyodontium album]]
+[[Category: Peptidase K]]
+[[Category: Gallagher-Jones, M]]
+[[Category: Glynn, C]]
+[[Category: Gonen, T]]
+[[Category: Hattne, J]]
+[[Category: Martynowycz, M W]]
+[[Category: Rodriguez, J A]]
+[[Category: Shi, D]]
+[[Category: Zee, C T]]
+[[Category: Hydrolase]]