6ZGL
Structure of DPS determined by movement-free cryoEM with zero dose extrapolation
Summary for 6ZGL
| Entry DOI | 10.2210/pdb6zgl/pdb |
| EMDB information | 11210 |
| Descriptor | DNA protection during starvation protein (2 entities in total) |
| Functional Keywords | dna-binding protein, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 12 |
| Total formula weight | 224643.54 |
| Authors | Naydenova, K.,Russo, C.J. (deposition date: 2020-06-19, release date: 2020-10-21, Last modification date: 2024-05-01) |
| Primary citation | Naydenova, K.,Jia, P.,Russo, C.J. Cryo-EM with sub-1 angstrom specimen movement. Science, 370:223-226, 2020 Cited by PubMed Abstract: Most information loss in cryogenic electron microscopy (cryo-EM) stems from particle movement during imaging, which remains poorly understood. We show that this movement is caused by buckling and subsequent deformation of the suspended ice, with a threshold that depends directly on the shape of the frozen water layer set by the support foil. We describe a specimen support design that eliminates buckling and reduces electron beam-induced particle movement to less than 1 angstrom. The design allows precise foil tracking during imaging with high-speed detectors, thereby lessening demands on cryostage precision and stability. It includes a maximal density of holes, which increases throughput in automated cryo-EM without degrading data quality. Movement-free imaging allows extrapolation to a three-dimensional map of the specimen at zero electron exposure, before the onset of radiation damage. PubMed: 33033219DOI: 10.1126/science.abb7927 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.9 Å) |
Structure validation
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