ArticleActa crystallographica. Section F, Structural biology communications2015
Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish β2-microglobulin.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
β(2)-Microglobulin (β(2)m) noncovalently associates with the heavy chain of major histocompatibility complex class I (MHC I) molecules, which bind foreign antigen peptides to control the cytotoxic T lymphocyte (CTL) immune response. In contrast to mammals, there are distinct types of β(2)ms derived from two loci in a number of teleost species. In order to clarify the structures of the β(2)ms, the zebrafish (Danio rerio) β(2)ms Dare-β(2)m-I and Dare-β(2)m-II were expressed in Escherichia coli, purified and crystallized, and diffraction data were collected to 1.6 and 1.9 Å resolution, respectively. Both crystals belonged to space group P2(1)2(1)2(1). The unit-cell parameters were determined to be a = 38.2, b = 50.4, c = 50.9 Å for Dare-β(2)m-I and a = 38.9, b = 52.7, c = 65.8 Å for Dare-β(2)m-II. Each asymmetric unit was constituted of one molecule, with Matthews coefficients of 2.22 and 3.01 Å(3) Da(-1) and solvent contents of 45 and 59% for Dare-β(2)m-I and Dare-β(2)m-II, respectively. These two β(2)m structures will provide relevant information for further studies of the structures of the MHC I complex.
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