9n0g: Difference between revisions

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'''Unreleased structure'''


The entry 9n0g is ON HOLD  until Paper Publication
==Structure of proteinase K from energy-filtered MicroED data using a 10 eV slit width==
<StructureSection load='9n0g' size='340' side='right'caption='[[9n0g]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9n0g]] 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=9N0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9N0G 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]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=9n0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9n0g OCA], [https://pdbe.org/9n0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9n0g RCSB], [https://www.ebi.ac.uk/pdbsum/9n0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9n0g 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 ==
A favorable signal-to-noise ratio is essential for obtaining high-quality diffraction data in macromolecular electron crystallography. Inelastic scattering contributes significantly to the noise, reducing contrast between diffraction peaks and background, which complicates peak detection and compromises the accuracy of intensity integration. Energy filtering mitigates these challenges and enhances diffraction data quality by removing the inelastically scattered electrons, leading to reduced background noise and sharper Bragg peaks. Previously, we reported a substantial improvement in MicroED data quality and resolution with energy filtering. Here, we systematically evaluate the impact of different energy filter slit widths for optimal MicroED data collection. Data from proteinase K lamellae were collected using the 5, 10, and 20 eV energy filter slit widths. Our results show that the narrowest slit widths result in a stronger diffraction signal with lower background noise, improving the precision of the intensity measurements which resulted in better structural models. Our findings provide insights into the optimization of energy filter slit settings that, when paired with direct electron detection, enhance MicroED data collection strategies in MicroED by improving the signal-to-noise ratio, supporting higher quality data and ultimately enabling more precise structure determination.


Authors:  
Characterization of energy filtering slit widths for MicroED data collection.,Clabbers MTB, Hattne J, Martynowycz MW, Gonen T bioRxiv [Preprint]. 2025 Feb 27:2025.02.24.639939. doi: , 10.1101/2025.02.24.639939. PMID:40060527<ref>PMID:40060527</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 9n0g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Parengyodontium album]]
[[Category: Clabbers MTB]]
[[Category: Gonen T]]
[[Category: Hattne J]]
[[Category: Martynowycz MW]]

Latest revision as of 20:00, 29 July 2026

Structure of proteinase K from energy-filtered MicroED data using a 10 eV slit width

9n0g, resolution 1.20Å

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