Open AccessCrystallization and preliminary X‐ray diffraction analysis of the β subunit Yke2 of the Gim complex from Saccharomyces cerevisiae
Author(s) -
Pérez de Diego Rebeca,
OrtizLombardía Miguel,
Bravo Jerónimo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108011846
Subject(s) - crystallization , saccharomyces cerevisiae , protein subunit , crystallography , diffraction , x ray crystallography , materials science , chemistry , biochemistry , physics , optics , yeast , gene , organic chemistry
The Gim complex (GimC) from Saccharomyces cerevisiae is a heterohexameric protein complex, also known as prefoldin (PFD), which binds and stabilizes unfolded target polypeptides and subsequently delivers them to chaperonins for completion of folding. In this study, the crystallization and preliminary X‐ray analysis of one of the β subunits of the Gim complex (Yke2) from S. cerevisiae are described. The purified protein was crystallized by the vapour‐diffusion method, producing two types of crystals that belonged to the orthorhombic space group C 222 or the primitive monoclinic space group P 2 1 . The unit‐cell parameters for the C ‐centred orthorhombic crystal were a = 48.2, b = 168.86, c = 131.81 Å and the unit‐cell parameters for the primitive monoclinic crystal were a = 47.83, b = 134.90, c = 81.50 Å, β = 100.71°. The Yke2 crystals diffracted to 4.2 and 3.1 Å resolution, respectively, on a rotating‐anode generator under cryoconditions. This is the first report concerning the crystallization of a β subunit of a eukaryotic prefoldin.