Open AccessCrystallization of the flexible nuclear import receptor importin‐β in the unliganded state
Author(s) -
Roman Noelia,
Kirkby Brenda,
Marfori Mary,
Kobe Bostjan,
Forwood Jade K.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109016820
Subject(s) - importin , nuclear pore , nuclear transport , cytoplasm , crystallization , crystallography , nucleus , molecule , biophysics , chemistry , macromolecule , cell nucleus , microbiology and biotechnology , biology , biochemistry , organic chemistry
The transport of macromolecules across the nuclear envelope is an essential eukaryotic process that enables proteins such as transcription factors, polymerases and histones to gain access to the genetic material contained within the nucleus. Importin‐β plays a central role in the nucleocytoplasmic transport process, mediating nuclear import through a range of interactions with cytoplasmic, nuclear and nuclear pore proteins such as importin‐α, Ran, nucleoporins and various cargo molecules. The unliganded form of the full‐length yeast importin‐β has been expressed and crystallized. The crystals were obtained by vapour diffusion at pH 6.5 and 290 K. The crystals belonged to space group P 2 1 (unit‐cell parameters a = 58.17, b = 127.25, c = 68.52 Å, β = 102.23). One molecule is expected in the asymmetric unit. The crystals diffracted to 2.4 Å resolution using a laboratory X‐ray source and were suitable for crystal structure determination.