Crystals of the Escherichia coli replication terminator protein (Tus) com- plexed with its binding site DNA were obtained by a microdialysis method using PEG 4000. They belong to the tetragonal space group P4,2,2 or P4,2,2 with the unit cell parameter: a = 68.1 A, c = 230.7 A and contain one protein
Crystallization and preliminary X-ray diffraction analysis of importin-α complexed with NLS peptidomimetics
✍ Scribed by Marcos R.M. Fontes; Trazel Teh; Ryan D. Riell; Seung Bum Park; Robert F. Standaert; Bostjan Kobe
- Publisher
- Elsevier Science
- Year
- 2005
- Tongue
- English
- Weight
- 200 KB
- Volume
- 1750
- Category
- Article
- ISSN
- 1570-9639
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✦ Synopsis
Importin-alpha is the nuclear import receptor that recognizes cargo proteins with nuclear localization sequences (NLSs). The study of NLS peptidomimetics can provide a better understanding of the requirements for the molecular recognition of cargo proteins by importin-alpha, and potentially engender a large number of applications in medicine. Importin-alpha was crystallized with a set of six NLS peptidomimetics, and X-ray diffraction data were collected in the range 2.1-2.5 A resolution. Preliminary electron density calculations show that the ligands are present in the crystals.
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