Determining structures in a native environment using single-particle cryoelectron microscopy images

Cryo-electron tomography is a powerful tool for structure determination in the native environment. However, this method requires the acquisition of tilt series, which is time-consuming and severely slows structure determination. By treating the densities of non-target protein as non-Gaussian noise,...

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Autores principales:	Jing Cheng, Bufan Li, Long Si, Xinzheng Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	cryo-EM native structure weighting function Science (General) Q1-390
Acceso en línea:	https://doaj.org/article/982c8e8ac97244f285df3c95b4c10043
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id	oai:doaj.org-article:982c8e8ac97244f285df3c95b4c10043
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spelling	oai:doaj.org-article:982c8e8ac97244f285df3c95b4c100432021-11-28T04:39:06ZDetermining structures in a native environment using single-particle cryoelectron microscopy images2666-675810.1016/j.xinn.2021.100166https://doaj.org/article/982c8e8ac97244f285df3c95b4c100432021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2666675821000916https://doaj.org/toc/2666-6758Cryo-electron tomography is a powerful tool for structure determination in the native environment. However, this method requires the acquisition of tilt series, which is time-consuming and severely slows structure determination. By treating the densities of non-target protein as non-Gaussian noise, we developed a new target function that greatly improves the efficiency of recognizing the target protein in a single cryo-electron microscopy image. Moreover, we developed a sorting function that effectively eliminates the model dependence and improved the resolution during the subsequent structure refinement procedure. By eliminating model bias, our method allows using homolog proteins as models to recognize the target proteins in a complex context. Together, we developed an in situ single-particle analysis method. Our method was successfully applied to solve structures of glycoproteins on the surface of a non-icosahedral virus and Rubisco inside the carboxysome. Both data were collected within 24 h, thus allowing fast and simple structural determination.Jing ChengBufan LiLong SiXinzheng ZhangElsevierarticlecryo-EMnative structureweighting functionScience (General)Q1-390ENThe Innovation, Vol 2, Iss 4, Pp 100166- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	cryo-EM native structure weighting function Science (General) Q1-390
spellingShingle	cryo-EM native structure weighting function Science (General) Q1-390 Jing Cheng Bufan Li Long Si Xinzheng Zhang Determining structures in a native environment using single-particle cryoelectron microscopy images
description	Cryo-electron tomography is a powerful tool for structure determination in the native environment. However, this method requires the acquisition of tilt series, which is time-consuming and severely slows structure determination. By treating the densities of non-target protein as non-Gaussian noise, we developed a new target function that greatly improves the efficiency of recognizing the target protein in a single cryo-electron microscopy image. Moreover, we developed a sorting function that effectively eliminates the model dependence and improved the resolution during the subsequent structure refinement procedure. By eliminating model bias, our method allows using homolog proteins as models to recognize the target proteins in a complex context. Together, we developed an in situ single-particle analysis method. Our method was successfully applied to solve structures of glycoproteins on the surface of a non-icosahedral virus and Rubisco inside the carboxysome. Both data were collected within 24 h, thus allowing fast and simple structural determination.
format	article
author	Jing Cheng Bufan Li Long Si Xinzheng Zhang
author_facet	Jing Cheng Bufan Li Long Si Xinzheng Zhang
author_sort	Jing Cheng
title	Determining structures in a native environment using single-particle cryoelectron microscopy images
title_short	Determining structures in a native environment using single-particle cryoelectron microscopy images
title_full	Determining structures in a native environment using single-particle cryoelectron microscopy images
title_fullStr	Determining structures in a native environment using single-particle cryoelectron microscopy images
title_full_unstemmed	Determining structures in a native environment using single-particle cryoelectron microscopy images
title_sort	determining structures in a native environment using single-particle cryoelectron microscopy images
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/982c8e8ac97244f285df3c95b4c10043
work_keys_str_mv	AT jingcheng determiningstructuresinanativeenvironmentusingsingleparticlecryoelectronmicroscopyimages AT bufanli determiningstructuresinanativeenvironmentusingsingleparticlecryoelectronmicroscopyimages AT longsi determiningstructuresinanativeenvironmentusingsingleparticlecryoelectronmicroscopyimages AT xinzhengzhang determiningstructuresinanativeenvironmentusingsingleparticlecryoelectronmicroscopyimages
_version_	1718408274301157376

Determining structures in a native environment using single-particle cryoelectron microscopy images

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