7n2h: Difference between revisions
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The | ==X-Ray structure of a sequence variant of a repeat segment of the yeast prion New1p== | ||
<StructureSection load='7n2h' size='340' side='right'caption='[[7n2h]], [[Resolution|resolution]] 1.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7n2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N2H FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.102Å</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=7n2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n2h OCA], [https://pdbe.org/7n2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n2h RCSB], [https://www.ebi.ac.uk/pdbsum/7n2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n2h ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Electron diffraction (MicroED/3DED) can render the three-dimensional atomic structures of molecules from previously unamenable samples. The approach has been particularly transformative for peptidic structures, where MicroED has revealed novel structures of naturally occurring peptides, synthetic protein fragments, and peptide-based natural products. Despite its transformative potential, MicroED is beholden to the crystallographic phase problem, which challenges its de novo determination of structures. ARCIMBOLDO, an automated, fragment-based approach to structure determination, eliminates the need for atomic resolution, instead enforcing stereochemical constraints through libraries of small model fragments, and discerning congruent motifs in solution space to ensure validation. This approach expands the reach of MicroED to presently inaccessible peptide structures including fragments of human amyloids, and yeast and mammalian prions. For electron diffraction, fragment-based phasing portends a more general phasing solution with limited model bias for a wider set of chemical structures. | |||
Fragment-Based Ab Initio Phasing of Peptidic Nanocrystals by MicroED.,Richards LS, Flores MD, Millan C, Glynn C, Zee CT, Sawaya MR, Gallagher-Jones M, Borges RJ, Uson I, Rodriguez JA ACS Bio Med Chem Au. 2023 Feb 23;3(2):201-210. doi: , 10.1021/acsbiomedchemau.2c00082. eCollection 2023 Apr 19. PMID:37096030<ref>PMID:37096030</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7n2h" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Richards | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Flores MD]] | |||
[[Category: Gallagher-Jones M]] | |||
[[Category: Glynn C]] | |||
[[Category: Richards LS]] | |||
[[Category: Sawaya MR]] | |||
[[Category: Zee CT]] | |||
Latest revision as of 13:40, 22 May 2024
X-Ray structure of a sequence variant of a repeat segment of the yeast prion New1pX-Ray structure of a sequence variant of a repeat segment of the yeast prion New1p
Structural highlights
Publication Abstract from PubMedElectron diffraction (MicroED/3DED) can render the three-dimensional atomic structures of molecules from previously unamenable samples. The approach has been particularly transformative for peptidic structures, where MicroED has revealed novel structures of naturally occurring peptides, synthetic protein fragments, and peptide-based natural products. Despite its transformative potential, MicroED is beholden to the crystallographic phase problem, which challenges its de novo determination of structures. ARCIMBOLDO, an automated, fragment-based approach to structure determination, eliminates the need for atomic resolution, instead enforcing stereochemical constraints through libraries of small model fragments, and discerning congruent motifs in solution space to ensure validation. This approach expands the reach of MicroED to presently inaccessible peptide structures including fragments of human amyloids, and yeast and mammalian prions. For electron diffraction, fragment-based phasing portends a more general phasing solution with limited model bias for a wider set of chemical structures. Fragment-Based Ab Initio Phasing of Peptidic Nanocrystals by MicroED.,Richards LS, Flores MD, Millan C, Glynn C, Zee CT, Sawaya MR, Gallagher-Jones M, Borges RJ, Uson I, Rodriguez JA ACS Bio Med Chem Au. 2023 Feb 23;3(2):201-210. doi: , 10.1021/acsbiomedchemau.2c00082. eCollection 2023 Apr 19. PMID:37096030[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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