In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 71, No. 12 ( 2015-12-01), p. 1481-1487
Abstract:
High conformational flexibility is an intrinsic and indispensable property of nuclear transport receptors, which makes crystallization and structure determination of macromolecular complexes containing exportins or importins particularly challenging. Here, the crystallization and structure determination of a quaternary nuclear export complex consisting of the exportin CRM1, the small GTPase Ran in its GTP-bound form, the export cargo SPN1 and an FG repeat-containing fragment of the nuclear pore complex component nucleoporin Nup214 fused to maltose-binding protein is reported. Optimization of constructs, seeding and the development of a sophisticated protocol including successive PEG-mediated crystal dehydration as well as additional post-mounting steps were essential to obtain well diffracting crystals.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X15021524
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2015
detail.hit.zdb_id:
2175956-X
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