Purification, Crystallization and Preliminary X-ray Analysis of Murine Interleukin-5
| Autor: | Amechand Boodhoo, Randy J. Read, Norma E.C. Duke, Mabel W.L. Ritzel, Dennis Kunimoto, Dequan Kong |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Stereochemistry
Glutamine Dimer Crystallography X-Ray law.invention Crystal Mice chemistry.chemical_compound X-Ray Diffraction Structural Biology law Animals Isoelectric Point Crystallization Molecular Biology Chemistry Resolution (electron density) Crystallography Isoelectric point X-ray crystallography Mutagenesis Site-Directed Orthorhombic crystal system Asparagine Interleukin-5 Protein crystallization Baculoviridae |
| Zdroj: | Journal of Molecular Biology. 241:269-272 |
| ISSN: | 0022-2836 |
| Popis: | Wild-type and mutant forms of murine interleukin-5 (mIL-5) have been expressed in the baculovirus expression system, purified, and used in crystallization trials. Attempts to obtain diffraction quality crystals of wild-type protein were unsuccessful. The substitution of glutamine for Asn75 preserved biological activity, while removing one of two predicted N-linked glycosylation sites, and the resulting protein was crystallized from polyethylene glycol 8000 at pH 7.8 in two crystal forms. The orthorhombic crystals, which belong to space group P2(1)2(1)2 with cell dimensions a = 55.9 A, b = 83.0 A and c = 52.3 A, diffract to beyond 2.5 A resolution. The second crystal form belongs to a trigonal space group, either P3(1)21 or P3(2)21, with cell dimensions a = b = 62.1 A, c = 129.9 A, and diffracts to about 3.8 A resolution. Each crystal form probably contains one mIL-5 dimer per asymmetric unit. |
| Databáze: | OpenAIRE |
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