Structural highlights
Function
DHE3_BOVIN May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).[1]
Publication Abstract from PubMed
For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions.
Addressing compressive deformation of proteins embedded in crystalline ice.,Shi H, Wu C, Zhang X Structure. 2022 Dec 14:S0969-2126(22)00487-7. doi: 10.1016/j.str.2022.12.001. PMID:36586403[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim DW, Eum WS, Jang SH, Yoon CS, Kim YH, Choi SH, Choi HS, Kim SY, Kwon HY, Kang JH, Kwon OS, Cho SW, Park J, Choi SY. Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase. J Biochem Mol Biol. 2003 Nov 30;36(6):545-51. PMID:14659072 doi:<ARTICLE_ID IdType=doi> <ARTICLE_ID IdType=doi>
- ↑ Shi H, Wu C, Zhang X. Addressing compressive deformation of proteins embedded in crystalline ice. Structure. 2022 Dec 14:S0969-2126(22)00487-7. doi: 10.1016/j.str.2022.12.001. PMID:36586403 doi:http://dx.doi.org/10.1016/j.str.2022.12.001
