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Autori principali: Li, Jianxun, Li, Tianpei, Wang, Saimeng, Zhang, Yu-Zhong, Liu, Lu-Ning, Wang, Peng
Natura: Artículo científico
Lingua:en
Pubblicazione: Plant physiology 2025
Accesso online:https://pubmed.ncbi.nlm.nih.gov/40341945/
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author Li, Jianxun
Li, Tianpei
Wang, Saimeng
Zhang, Yu-Zhong
Liu, Lu-Ning
Wang, Peng
author_facet Li, Jianxun
Li, Tianpei
Wang, Saimeng
Zhang, Yu-Zhong
Liu, Lu-Ning
Wang, Peng
Li, Jianxun
Li, Tianpei
Wang, Saimeng
Zhang, Yu-Zhong
Liu, Lu-Ning
Wang, Peng
collection PubMed - marine biology
contents Symmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the α-carboxysome shell. Li, Jianxun Li, Tianpei Wang, Saimeng Zhang, Yu-Zhong Liu, Lu-Ning Wang, Peng Excessive symmetry in cryo-EM data processing can distort key structural details of bacterial microcompartments, highlighting the importance of balanced symmetry for accurate structural insights.
format Artículo científico
id pubmed_40341945
institution PubMed
language en
publishDate 2025
publisher Plant physiology
record_format pubmed
spellingShingle Symmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the α-carboxysome shell.
Li, Jianxun
Li, Tianpei
Wang, Saimeng
Zhang, Yu-Zhong
Liu, Lu-Ning
Wang, Peng
Symmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the α-carboxysome shell. Li, Jianxun Li, Tianpei Wang, Saimeng Zhang, Yu-Zhong Liu, Lu-Ning Wang, Peng Excessive symmetry in cryo-EM data processing can distort key structural details of bacterial microcompartments, highlighting the importance of balanced symmetry for accurate structural insights.
title Symmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the α-carboxysome shell.
url https://pubmed.ncbi.nlm.nih.gov/40341945/