Crystallization and Preliminary X-Ray Diffraction Analysis of the ZAD Domain of the Serendipity-d Protein from Drosophila melanogaster

Abstract

The spatial organization of the genome is controlled by a special class of architectural proteins, in particular proteins containing ZAD domains that are able to form homo- and heterodimers. These domains are unique for arthropods and are present at the N-terminus of many proteins containing C2H2-type zinc fingers. Despite a growing interest in the characterization of architectural proteins, little is known about their structures (structures of their functional domains), which could shed light on the mechanisms of regulatory processes of the establishment and maintenance of the spatial organization of chromatin domains. Only two structures of ZAD domains are known. Here we report the crystallization and preliminary X-ray diffraction analysis of the previously unknown ZAD domain of the Serendipity-d protein from Drosophila melanogaster.