Structural highlights
Function
THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
Publication Abstract from PubMed
Traditionally, crystallographic analysis of macromolecules has depended on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from pathologies that render them inappropriate for high-resolution structure determination. Here we show that fragmentation of large, imperfect crystals into microcrystals or nanocrystals can provide a simple path for high-resolution structure determination by the cryoEM method MicroED and potentially by serial femtosecond crystallography.
Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.,de la Cruz MJ, Hattne J, Shi D, Seidler P, Rodriguez J, Reyes FE, Sawaya MR, Cascio D, Weiss SC, Kim SK, Hinck CS, Hinck AP, Calero G, Eisenberg D, Gonen T Nat Methods. 2017 Feb 13;14(4):399-402. doi: 10.1038/nmeth.4178. PMID:28192420[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de la Cruz MJ, Hattne J, Shi D, Seidler P, Rodriguez J, Reyes FE, Sawaya MR, Cascio D, Weiss SC, Kim SK, Hinck CS, Hinck AP, Calero G, Eisenberg D, Gonen T. Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. Nat Methods. 2017 Feb 13;14(4):399-402. doi: 10.1038/nmeth.4178. PMID:28192420 doi:http://dx.doi.org/10.1038/nmeth.4178