5K7Q

MicroED structure of thaumatin at 2.5 A resolution

Summary for 5K7Q

• Entry DOI: 10.2210/pdb5k7q/pdb
• Related: 5K7N 5K7O 5K7P 5K7R 5K7S 5K7T
• EMDB information: 8216 8217 8218 8219 8220 8221 8222
• Descriptor: Thaumatin-1 (2 entities in total)
• Functional Keywords: sweet protein, plant protein
• Biological source: Thaumatococcus daniellii (Katemfe)
• Total number of polymer chains: 1
• Total formula weight: 22227.06

Authors

de la Cruz, M.J.,Hattne, J.,Shi, D.,Seidler, P.,Rodriguez, J.,Reyes, F.E.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.,Gonen, T. (deposition date: 2016-05-26, release date: 2017-04-05, Last modification date: 2024-11-13)

Primary citation

de la Cruz, M.J.,Hattne, J.,Shi, D.,Seidler, P.,Rodriguez, J.,Reyes, F.E.,Sawaya, M.R.,Cascio, D.,Weiss, S.C.,Kim, S.K.,Hinck, C.S.,Hinck, A.P.,Calero, G.,Eisenberg, D.,Gonen, T.
Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.
Nat. Methods, 14:399-402, 2017

PubMed Abstract: 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.

PubMed: 28192420
DOI: 10.1038/nmeth.4178

Experimental method

ELECTRON CRYSTALLOGRAPHY (2.5 Å)