title: Crystallization and preliminary X-ray crystallographic analysis of SEDL.
abstract: SEDL (known also as sedlin) is a 140 amino-acid protein with a putative role in endoplasmic reticulum-to-Golgi transport. Several missense mutations and deletion mutations in the SEDL gene, which result in protein truncation by frame shift, are responsible for spondyloepiphyseal dysplasia tarda, a progressive skeletal disorder. The protein is identical to MIP-2A, which was shown to interact physically with c-myc promotor-binding protein 1 (MBP-1) and relieve the regulatory role of MBP-1 as a general transcription repressor. In order to gain insights into the function of SEDL by structural analysis, the protein was overexpressed and crystallized as a first step. SEDL was overexpressed in Escherichia coli and crystallized using the hanging-drop vapour-diffusion method at 298 K. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 46.69, b = 101.30, c = 66.15 A. The unit cell is likely to contain one molecule of SEDL, with a crystal volume per protein mass (V(M)) of 2.36 A(3)Da(-1) and a solvent content of about 47.9% by volume. A native data set to 2.8 A resolution was obtained from a flash-cooled crystal using synchrotron radiation.
authors.affiliation: National Creative Research Initiative Center for Biomolecular Recognition and Department of Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, South Korea.
authors.forename: Se Bok
authors.initials: SB
authors.lastname: Jang
authors.forename: Yong-Soon
authors.initials: YS
authors.lastname: Cho
authors.forename: Soo-Jung
authors.initials: SJ
authors.lastname: Eom
authors.forename: Eui-Ju
authors.initials: EJ
authors.lastname: Choi
authors.forename: Kyung-Hwa
authors.initials: KH
authors.lastname: Kim
authors.forename: Pann-Ghill
authors.initials: PG
authors.lastname: Suh
authors.forename: Byung-Ha
authors.initials: BH
authors.lastname: Oh
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D026901:Membrane Transport Proteins; D051379:Mice; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013045:Species Specificity; D014157:Transcription Factors
chemical_list: D002352:Carrier Proteins; D026901:Membrane Transport Proteins; D011994:Recombinant Proteins; C120759:TRAPPC2 protein, human; D014157:Transcription Factors