<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>62</viewCount><searchCount>0</searchCount></scores><additional><submitter>Bajaj CL</submitter><funding>NIBIB NIH HHS</funding><funding>NCRR NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>236-239</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2678009</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>2007</volume><pubmed_abstract>Three dimensional Electron Microscopy (EM) and in particular single particle reconstruction using cryo-EM, has rapidly advanced over recent years, such that increasingly several macromolecular complexes can be resolved at subnanometer resolution (6-10 Å). This paper reviews some of the main volumetric image and geometric post-processing steps once a three dimensional EM map (henceforth a 3D map) has been reconstructed from single particle Cryo-EM, as essential steps in an enhanced and automated computational structure interpretation pipeline. In particular the paper addresses automated filtering, critical point calculations, symmetric and non-symmetric molecular domain segmentation, molecular surface selection, curation, and protein secondary structure (α- helices and β-sheets) elucidation from 3D maps.</pubmed_abstract><journal>Proceedings. IEEE International Symposium on Biomedical Imaging</journal><pubmed_title>AUTOMATIC STRUCTURE INTERPRETATION OF SINGLE PARTICLE CRYO-ELECTRON MICROSCOPY: FROM IMAGES TO PSUEDO-ATOMIC MODELS.</pubmed_title><pmcid>PMC2678009</pmcid><funding_grant_id>P41 RR008605-147784</funding_grant_id><funding_grant_id>R01 EB004873-01A2</funding_grant_id><funding_grant_id>R01 GM073087-01A1</funding_grant_id><funding_grant_id>P41 RR002250-200095</funding_grant_id><funding_grant_id>R01 GM074258-02</funding_grant_id><funding_grant_id>R01 GM073087</funding_grant_id><funding_grant_id>R01 GM074258-03</funding_grant_id><funding_grant_id>P41 RR008605-147779</funding_grant_id><funding_grant_id>P41 RR008605-158490</funding_grant_id><funding_grant_id>R01 GM073087-03</funding_grant_id><funding_grant_id>P41 RR008605</funding_grant_id><funding_grant_id>R01 GM073087-02</funding_grant_id><funding_grant_id>R01 GM074258-01</funding_grant_id><funding_grant_id>P41 RR002250-217415</funding_grant_id><funding_grant_id>P41 RR008605-158485</funding_grant_id><funding_grant_id>P41 RR002250</funding_grant_id><funding_grant_id>R01 GM074258</funding_grant_id><funding_grant_id>P41 RR002250-226519</funding_grant_id><funding_grant_id>R01 EB004873</funding_grant_id><funding_grant_id>R01 EB004873-02</funding_grant_id><funding_grant_id>P20 RR020647</funding_grant_id><pubmed_authors>Bajaj CL</pubmed_authors><view_count>62</view_count></additional><is_claimable>false</is_claimable><name>AUTOMATIC STRUCTURE INTERPRETATION OF SINGLE PARTICLE CRYO-ELECTRON MICROSCOPY: FROM IMAGES TO PSUEDO-ATOMIC MODELS.</name><description>Three dimensional Electron Microscopy (EM) and in particular single particle reconstruction using cryo-EM, has rapidly advanced over recent years, such that increasingly several macromolecular complexes can be resolved at subnanometer resolution (6-10 Å). This paper reviews some of the main volumetric image and geometric post-processing steps once a three dimensional EM map (henceforth a 3D map) has been reconstructed from single particle Cryo-EM, as essential steps in an enhanced and automated computational structure interpretation pipeline. In particular the paper addresses automated filtering, critical point calculations, symmetric and non-symmetric molecular domain segmentation, molecular surface selection, curation, and protein secondary structure (α- helices and β-sheets) elucidation from 3D maps.</description><dates><release>2007-01-01T00:00:00Z</release><publication>2007 Apr</publication><modification>2024-10-15T16:43:42.593Z</modification><creation>2019-03-27T00:22:11Z</creation></dates><accession>S-EPMC2678009</accession><cross_references><pubmed>19424455</pubmed><doi>10.1109/isbi.2007.356832</doi><doi>10.1109/ISBI.2007.356832</doi></cross_references></HashMap>