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
Crystallization and preliminary X-ray diffraction analysis of staphylococcal enterotoxin type C
β Scribed by Dr. Gregory A. Bohach; Young-In Chi; Cynthia V. Stauffacher
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 577 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0887-3585
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β¦ Synopsis
Abstract
The Type C staphylococcal enterotoxin produced by Staphylococcus aureus strain FRIβ909 has been crystallized using a combination of two precipitants, ammonium sulfate and polyethylene glycol 400, with the addition of small amounts of detergent. Two related crystal forms have been obtained, one triclinic, and one tetragonal, both with one toxin molecule per asymmetric unit. These crystals are stable for at least 75 hr in the Xβray beam and diffract to at least 2.2 and 2.6 Γ , respectively. The triclinic crystals have unit cell parameters a = 38.5 Γ , b = 43.7 Γ , c = 36.9 Γ , and interaxial angles Ξ± = 99.9Β°, Ξ² = 95.8Β°, and Ξ³ = 98.5Β°. The tetragonal crystals are of space group __P__4~1~22 with unit cell parameters a = 43.4 Γ and c = 278.0 Γ . Β© 1992 WileyβLiss, Inc.
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