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- 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-, Ran, nucleoporins and various cargo molecules. The unliganded form of the full-length yeast importin- 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 P21 (unit-cell parameters a = 58.17, b = 127.25, c = 68.52 Ã…, = 102.23). One molecule is expected in the asymmetric unit. The crystals diffracted to 2.4 Ã… resolution using a laboratory X-ray source and were suitable for crystal structure determination.
|Number of pages||4|
|Journal||Acta Crystallographica Section F:Structural Biology Communications|
|Publication status||Published - 2009|
Roman, N., Kirkby, B., Marfori, M., Kobe, B., & Forwood, J. (2009). Crystallization of the flexible nuclear import receptor importin-ÃŸ in the unliganded state. Acta Crystallographica Section F:Structural Biology Communications, 65(6), 625-628. https://doi.org/10.1107/S1744309109016820