Structural highlights
Function
[ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]
Publication Abstract from PubMed
Nearly all single-particle cryo-EM structures resolved to better than 4-A resolution have been determined using 300-keV transmission electron microscopes (TEMs). We demonstrate that it is possible to obtain reconstructions of macromolecular complexes of different sizes to better than 3-A resolution using a 200-keV TEM. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules.
Achieving better-than-3-A resolution by single-particle cryo-EM at 200 keV.,Herzik MA Jr, Wu M, Lander GC Nat Methods. 2017 Oct 9. doi: 10.1038/nmeth.4461. PMID:28991891[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ St-Jean M, Izard T, Sygusch J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. J Biol Chem. 2007 May 11;282(19):14309-15. Epub 2007 Feb 27. PMID:17329259 doi:10.1074/jbc.M611505200
- ↑ Herzik MA Jr, Wu M, Lander GC. Achieving better-than-3-A resolution by single-particle cryo-EM at 200 keV. Nat Methods. 2017 Oct 9. doi: 10.1038/nmeth.4461. PMID:28991891 doi:http://dx.doi.org/10.1038/nmeth.4461
