Flexible workflows for on-the-fly electronmicroscopy single-particle image processing using Scipion

Electron microscopy of macromolecular structures is an approach that is in increasing demand in the field of structural biology. The automation of image acquisition has greatly increased the potential throughput of electron microscopy. Here, the focus is on the possibilities in Scipion to implement...

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Detalles Bibliográficos
Autores: Maluenda, D., Majtner, T., Horvath, P., Vilas, J.L., Jiménez-Moreno, A., Mota, J., Ramírez-Aportela, E., Sánchez-García, R., Conesa, P., Caño, L. del, Rancel, Y., Fonseca, Y., Martínez, M., Sharov, G., García, C.A., Strelak, D., Melero, R., Marabini Ruiz, Roberto, Carazo, J.M., Sorzano, C.O.S.
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/690936
Acceso en línea:http://hdl.handle.net/10486/690936
https://dx.doi.org/10.1107/S2059798319011860
Access Level:acceso abierto
Palabra clave:Scipion
image processing
electron microscopy
single-particle analysis
stream processing
electron-microscopy facilities
Biología y Biomedicina / Biología
Descripción
Sumario:Electron microscopy of macromolecular structures is an approach that is in increasing demand in the field of structural biology. The automation of image acquisition has greatly increased the potential throughput of electron microscopy. Here, the focus is on the possibilities in Scipion to implement flexible and robust image-processing workflows that allow the electron-microscope operator and the user to monitor the quality of image acquisition, assessing very simple acquisition measures or obtaining a first estimate of the initial volume, or the data resolution and heterogeneity, without any need for programming skills. These workflows can implement intelligent automatic decisions and they can warn the user of possible acquisition failures. These concepts are illustrated by analysis of the well known 2.2 Å resolution β-galactosidase data set