Purification, crystallization and preliminary crystallographic data of the m(3)G cap-binding domain of human snRNP import factor snurportin 1
2004 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Purification, crystallization and preliminary crystallographic data of the m(3)G cap-binding domain of human snRNP import factor snurportin 1
Strasser, A.; Dickmanns, A. ; Schmidt, U.; Penka, E.; Urlaub, H. ; Sekine, M. & Luhrmann, R. et al. (2004)
Acta Crystallographica Section D Biological Crystallography, 60 pp. 1628-1631. DOI: https://doi.org/10.1107/S0907444904015380
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- Authors
- Strasser, A.; Dickmanns, A. ; Schmidt, U.; Penka, E.; Urlaub, H. ; Sekine, M.; Luhrmann, R.; Ficner, R.
- Abstract
- The nuclear import of spliceosomal UsnRNPs is mediated by the transport adaptor snurportin 1 (SPN1), which specifically recognizes the 2,2,7-trimethylguanosine (m(3)G) cap at the 5' end of UsnRNAs. Human SPN1 was overexpressed as a GST-fusion protein in Escherichia coli and purified to homogeneity Since full-length SPN1 did not crystallize, limited proteolysis experiments were performed and stable digestion products were analyzed for functionality with respect to m(3)G cap-binding activity and subsequently used for crystallization trials. Well diffracting single crystals of a truncated SPN1 m(3)G cap-binding domain (residues 79-300) were obtained after two rounds of seeding. The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 57.47, c = 130.09 Angstrom, alpha = beta = gamma = 90degrees. Crystals contain one molecule in the asymmetric unit and diffract to a resolution limit of 2.9 Angstrom.
- Issue Date
- 2004
- Journal
- Acta Crystallographica Section D Biological Crystallography
- ISSN
- 0907-4449