2QEL: Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein

The use of high temperatures in the purification procedures of heat-stable proteins is a well established technique. Recently, rapid pre-heat treatment of protein samples prior to crystallization trials was described as a final polishing step to improve the diffraction properties of crystals [Pusey et al. (2005), Prog. Biophys. Mol. Biol. 88, 359-386]. The present study demonstrates that extended high-temperature incubation (328 K for 48 h) of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S successfully removes heterogeneities and allows the reproducible growth of well diffracting crystals. Heat treatment might be applied as an optimization method to other cases in which the protein/biomolecule fails to form diffracting crystals.
PDB ID: 2QELDownload
MMDB ID: 59447
PDB Deposition Date: 2007/6/26
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.29  Å
Source Organism:
Similar Structures:
Biological Unit for 2QEL: tetrameric; determined by author and by software (PISA)
Molecular Components in 2QEL
Label Count Molecule
Proteins (4 molecules)
Transthyretin(Gene symbol: TTR)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB