2YNJ
GroEL at sub-nanometer resolution by Constrained Single Particle Tomography
Summary for 2YNJ
Entry DOI | 10.2210/pdb2ynj/pdb |
EMDB information | 2221 |
Descriptor | 60 KDA CHAPERONIN, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, THALLIUM (I) ION, ... (4 entities in total) |
Functional Keywords | chaperone |
Biological source | ESCHERICHIA COLI UTI89 |
Cellular location | Cytoplasm : Q1R3B6 |
Total number of polymer chains | 14 |
Total formula weight | 792192.65 |
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 citation | Bartesaghi, 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: 23217682DOI: 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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