8VY3
Human DNA polymerase alpha/primase - AavLEA1 (1:40 molar ratio)
Summary for 8VY3
| Entry DOI | 10.2210/pdb8vy3/pdb |
| EMDB information | 43628 |
| Descriptor | DNA primase small subunit, DNA primase large subunit, DNA polymerase alpha catalytic subunit, ... (6 entities in total) |
| Functional Keywords | human dna poly alpha/primase, aavlea1, air-water-interface, replication |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 277624.90 |
| Authors | |
| Primary citation | Abe, K.M.,Li, G.,He, Q.,Grant, T.,Lim, C.J. Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing. Nat Commun, 15:7705-7705, 2024 Cited by PubMed Abstract: Air-water interface (AWI) interactions during cryo-electron microscopy (cryo-EM) sample preparation cause significant sample loss, hindering structural biology research. Organisms like nematodes and tardigrades produce Late Embryogenesis Abundant (LEA) proteins to withstand desiccation stress. Here we show that these LEA proteins, when used as additives during plunge freezing, effectively mitigate AWI damage to fragile multi-subunit molecular samples. The resulting high-resolution cryo-EM maps are comparable to or better than those obtained using existing AWI damage mitigation methods. Cryogenic electron tomography reveals that particles are localized at specific interfaces, suggesting LEA proteins form a barrier at the AWI. This interaction may explain the observed sample-dependent preferred orientation of particles. LEA proteins offer a simple, cost-effective, and adaptable approach for cryo-EM structural biologists to overcome AWI-related sample damage, potentially revitalizing challenging projects and advancing the field of structural biology. PubMed: 39231985DOI: 10.1038/s41467-024-52091-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.98 Å) |
Structure validation
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