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2YNJ

GroEL at sub-nanometer resolution by Constrained Single Particle Tomography

Summary for 2YNJ
Entry DOI10.2210/pdb2ynj/pdb
EMDB information2221
Descriptor60 KDA CHAPERONIN, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, THALLIUM (I) ION, ... (4 entities in total)
Functional Keywordschaperone
Biological sourceESCHERICHIA COLI UTI89
Cellular locationCytoplasm : Q1R3B6
Total number of polymer chains14
Total formula weight792192.65
Authors
Bartesaghi, A.,Lecumberry, F.,Sapiro, G.,Subramaniam, S. (deposition date: 2012-10-15, release date: 2012-12-12, Last modification date: 2024-05-08)
Primary citationBartesaghi, A.,Lecumberry, F.,Sapiro, G.,Subramaniam, S.
Protein Secondary Structure Determination by Constrained Single-Particle Cryo-Electron Tomography
Structure, 20:2003-, 2012
Cited by
PubMed Abstract: Cryo-electron microscopy (cryo-EM) is a powerful technique for 3D structure determination of protein complexes by averaging information from individual molecular images. The resolutions that can be achieved with single-particle cryo-EM are frequently limited by inaccuracies in assigning molecular orientations based solely on 2D projection images. Tomographic data collection schemes, however, provide powerful constraints that can be used to more accurately determine molecular orientations necessary for 3D reconstruction. Here, we propose "constrained single-particle tomography" as a general strategy for 3D structure determination in cryo-EM. A key component of our approach is the effective use of images recorded in tilt series to extract high-resolution information and correct for the contrast transfer function. By incorporating geometric constraints into the refinement to improve orientational accuracy of images, we reduce model bias and overrefinement artifacts and demonstrate that protein structures can be determined at resolutions of ∼8 Å starting from low-dose tomographic tilt series.
PubMed: 23217682
DOI: 10.1016/J.STR.2012.10.016
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.4 Å)
Structure validation

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