Loading…
Volta phase plate cryo-EM of the small protein complex Prx3
Content Partner: Lincoln University. Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure...
Saved in:
Main Authors: | , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Online Access: | Request full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | |
container_end_page | |
container_issue | |
container_start_page | |
container_title | |
container_volume | |
creator | Khoshouei, M Radjainia, M Phillips, Amy Gerrard, J. A Mitra, A. K Plitzko, J. M Baumeister, W Danev, R |
description | Content Partner: Lincoln University. Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure
depositions, particularly for relatively small particles ( |
format | article |
fullrecord | <record><control><sourceid>nlnz_DQSLZ</sourceid><recordid>TN_cdi_nlnz_digitalnz_v2_39722786</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>39722786</sourcerecordid><originalsourceid>FETCH-nlnz_digitalnz_v2_397227863</originalsourceid><addsrcrecordid>eNrjZLAOy88pSVQoyEgsTlUoyEksSVVILqrM13X1VchPUyjJSFUozk3MyVEoKMovSc3MU0jOzy3ISa1QCCiqMOZhYE1LzClO5YXS3AyKbq4hzh66eTl5VfEpmemZJYkgVplRvLGluZGRuYWZMTFqAGqBL7o</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Volta phase plate cryo-EM of the small protein complex Prx3</title><source>DigitalNZ</source><creator>Khoshouei, M ; Radjainia, M ; Phillips, Amy ; Gerrard, J. A ; Mitra, A. K ; Plitzko, J. M ; Baumeister, W ; Danev, R</creator><creatorcontrib>Khoshouei, M ; Radjainia, M ; Phillips, Amy ; Gerrard, J. A ; Mitra, A. K ; Plitzko, J. M ; Baumeister, W ; Danev, R</creatorcontrib><description>Content Partner: Lincoln University. Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure
depositions, particularly for relatively small particles (<400 kDa). Here we demonstrate the benefits of Volta phase plates for single-particle analysis by time-efficient cryo-EM structure determination of 257 kDa human peroxiredoxin-3 dodecamers at 4.4 Å resolution. The Volta phase plate improves the applicability of cryo-EM for small molecules and accelerates
structure determination.</description><language>eng</language><publisher>Nature Publishing Group</publisher><creationdate>2016-01</creationdate><rights>Some rights reserved</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>777,25575</link.rule.ids><linktorsrc>$$Uhttp://api.digitalnz.org/records/39722786/source$$EView_record_in_DigitalNZ$$FView_record_in_$$GDigitalNZ$$Hfree_for_read</linktorsrc></links><search><creatorcontrib>Khoshouei, M</creatorcontrib><creatorcontrib>Radjainia, M</creatorcontrib><creatorcontrib>Phillips, Amy</creatorcontrib><creatorcontrib>Gerrard, J. A</creatorcontrib><creatorcontrib>Mitra, A. K</creatorcontrib><creatorcontrib>Plitzko, J. M</creatorcontrib><creatorcontrib>Baumeister, W</creatorcontrib><creatorcontrib>Danev, R</creatorcontrib><title>Volta phase plate cryo-EM of the small protein complex Prx3</title><description>Content Partner: Lincoln University. Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure
depositions, particularly for relatively small particles (<400 kDa). Here we demonstrate the benefits of Volta phase plates for single-particle analysis by time-efficient cryo-EM structure determination of 257 kDa human peroxiredoxin-3 dodecamers at 4.4 Å resolution. The Volta phase plate improves the applicability of cryo-EM for small molecules and accelerates
structure determination.</description><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>DQSLZ</sourceid><recordid>eNrjZLAOy88pSVQoyEgsTlUoyEksSVVILqrM13X1VchPUyjJSFUozk3MyVEoKMovSc3MU0jOzy3ISa1QCCiqMOZhYE1LzClO5YXS3AyKbq4hzh66eTl5VfEpmemZJYkgVplRvLGluZGRuYWZMTFqAGqBL7o</recordid><startdate>20160128</startdate><enddate>20160128</enddate><creator>Khoshouei, M</creator><creator>Radjainia, M</creator><creator>Phillips, Amy</creator><creator>Gerrard, J. A</creator><creator>Mitra, A. K</creator><creator>Plitzko, J. M</creator><creator>Baumeister, W</creator><creator>Danev, R</creator><general>Nature Publishing Group</general><scope>DQSLZ</scope><scope>HAZOD</scope></search><sort><creationdate>20160128</creationdate><title>Volta phase plate cryo-EM of the small protein complex Prx3</title><author>Khoshouei, M ; Radjainia, M ; Phillips, Amy ; Gerrard, J. A ; Mitra, A. K ; Plitzko, J. M ; Baumeister, W ; Danev, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-nlnz_digitalnz_v2_397227863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><toplevel>online_resources</toplevel><creatorcontrib>Khoshouei, M</creatorcontrib><creatorcontrib>Radjainia, M</creatorcontrib><creatorcontrib>Phillips, Amy</creatorcontrib><creatorcontrib>Gerrard, J. A</creatorcontrib><creatorcontrib>Mitra, A. K</creatorcontrib><creatorcontrib>Plitzko, J. M</creatorcontrib><creatorcontrib>Baumeister, W</creatorcontrib><creatorcontrib>Danev, R</creatorcontrib><collection>DigitalNZ</collection><collection>DigitalNZ</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Khoshouei, M</au><au>Radjainia, M</au><au>Phillips, Amy</au><au>Gerrard, J. A</au><au>Mitra, A. K</au><au>Plitzko, J. M</au><au>Baumeister, W</au><au>Danev, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Volta phase plate cryo-EM of the small protein complex Prx3</atitle><date>2016-01-28</date><risdate>2016</risdate><abstract>Content Partner: Lincoln University. Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure
depositions, particularly for relatively small particles (<400 kDa). Here we demonstrate the benefits of Volta phase plates for single-particle analysis by time-efficient cryo-EM structure determination of 257 kDa human peroxiredoxin-3 dodecamers at 4.4 Å resolution. The Volta phase plate improves the applicability of cryo-EM for small molecules and accelerates
structure determination.</abstract><pub>Nature Publishing Group</pub><oa>free_for_read</oa></addata></record> |
fulltext | fulltext_linktorsrc |
identifier | |
ispartof | |
issn | |
language | eng |
recordid | cdi_nlnz_digitalnz_v2_39722786 |
source | DigitalNZ |
title | Volta phase plate cryo-EM of the small protein complex Prx3 |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T22%3A56%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-nlnz_DQSLZ&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Volta%20phase%20plate%20cryo-EM%20of%20the%20small%20protein%20complex%20Prx3&rft.au=Khoshouei,%20M&rft.date=2016-01-28&rft_id=info:doi/&rft_dat=%3Cnlnz_DQSLZ%3E39722786%3C/nlnz_DQSLZ%3E%3Cgrp_id%3Ecdi_FETCH-nlnz_digitalnz_v2_397227863%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |