Protein structure determination by electron cryo-microscopy.
Transmission electron cryo-microscopy (cryoEM) is a versatile tool in the structural analysis of proteins and biological macromolecular assemblies. In this review, we present a brief survey of the methods used in cryoEM, and their current developments. These latest advances provide exciting opportun...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2009
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| _version_ | 1797081625818824704 |
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| author | Jonic, S Vénien-Bryan, C |
| author_facet | Jonic, S Vénien-Bryan, C |
| author_sort | Jonic, S |
| collection | OXFORD |
| description | Transmission electron cryo-microscopy (cryoEM) is a versatile tool in the structural analysis of proteins and biological macromolecular assemblies. In this review, we present a brief survey of the methods used in cryoEM, and their current developments. These latest advances provide exciting opportunities for the three-dimensional structural determination of macromolecular complexes that are either too large or too heterogeneous to be investigated by conventional X-ray crystallography or nuclear magnetic resonance (NMR). The endeavour of understanding the function of protein or macromolecular complex is often helped by combining data from electron microscopy and X-ray crystallography. We will thus provide a brief overview of the computational techniques involved in combining data from different techniques for the interpretation of the EM structure. |
| first_indexed | 2024-03-07T01:16:49Z |
| format | Journal article |
| id | oxford-uuid:8ef83c1c-f2a7-4c27-b000-307e27dfe785 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:16:49Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:8ef83c1c-f2a7-4c27-b000-307e27dfe7852022-03-26T23:01:09ZProtein structure determination by electron cryo-microscopy.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8ef83c1c-f2a7-4c27-b000-307e27dfe785EnglishSymplectic Elements at Oxford2009Jonic, SVénien-Bryan, CTransmission electron cryo-microscopy (cryoEM) is a versatile tool in the structural analysis of proteins and biological macromolecular assemblies. In this review, we present a brief survey of the methods used in cryoEM, and their current developments. These latest advances provide exciting opportunities for the three-dimensional structural determination of macromolecular complexes that are either too large or too heterogeneous to be investigated by conventional X-ray crystallography or nuclear magnetic resonance (NMR). The endeavour of understanding the function of protein or macromolecular complex is often helped by combining data from electron microscopy and X-ray crystallography. We will thus provide a brief overview of the computational techniques involved in combining data from different techniques for the interpretation of the EM structure. |
| spellingShingle | Jonic, S Vénien-Bryan, C Protein structure determination by electron cryo-microscopy. |
| title | Protein structure determination by electron cryo-microscopy. |
| title_full | Protein structure determination by electron cryo-microscopy. |
| title_fullStr | Protein structure determination by electron cryo-microscopy. |
| title_full_unstemmed | Protein structure determination by electron cryo-microscopy. |
| title_short | Protein structure determination by electron cryo-microscopy. |
| title_sort | protein structure determination by electron cryo microscopy |
| work_keys_str_mv | AT jonics proteinstructuredeterminationbyelectroncryomicroscopy AT venienbryanc proteinstructuredeterminationbyelectroncryomicroscopy |