Year: 2011
Type: article
Abstract: Poster Sessions C480 like a tetramer.Ultracentrifugation and native PAGE results also do not conclusively show whether it is a trimer or tetramer [4].Initial crystallographic data however showed 3 molecules in the asymmetric unit suggesting an elongated trimer.SAXS scattering curve of the IgD binding domain is indicative of a trimeric arrangement and ab initio modeling confirms fibrous elongated shape.Recently circular dichroism spectroscopy was done on MID962-1200 and the data were deconvoluted using DICHROWEB [5].The analyzed data with good NRMSD value shows approximately 11% alpha helices, 32% beta sheets and 30% unordered secondary structure.We crystallized the protein MID962-1200 with His-tag at concentration 10 mg/ml, but had problem with reproducibility limiting our ability for experimental phasing.Now we have recloned it in pETM-30 with a cleavable GST-tag, which is digested by TEV protease [6] made in house, to allow for crystallization of the protein without any tag.The crystal structure of MID962-1200 domain alone and in complex with its partners like IgD will elucidate the mechanism of this protein and give information on host-pathogen interactions.
Authors: M. Allaire, A. S. Soares, M. A. Engel, R. Stearns, S. Datwani, J. Olechno, R. Ellson, A. Héroux, J. M. Skinner, A. M. Orville
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W2334575316