| Autor: |
Boodhoo, Amechand, Duke, Norma E.C., Kong, Dequan, Ritzel, Mabel W.L., Kunimoto, Dennis Y., Read, Randy J. |
| Zdroj: |
JMB Online (Journal of Molecular Biology); August 1994, Vol. 241 Issue: 2 p269-272, 4p |
| Abstrakt: |
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 P21212 with cell dimensions a=55·9 Å, b=83·0 Å and c=52·3 Å, diffract to beyond 2·5 Å resolution. The second crystal form belongs to a trigonal space group, either P3121 or P3221, with cell dimensions a=b=62·1 Å, c=129·9 Å, and diffracts to about 3·8 Å resolution. Each crystal form probably contains one MIL-5 dimer per asymmetric unit. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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