Crystallization and preliminary X-ray crystallographic analysis of SEDL
SCIE
SCOPUS
- Title
- Crystallization and preliminary X-ray crystallographic analysis of SEDL
- Authors
- Jang, SB; Cho, YS; Eom, SJ; Choi, EJ; Kim, KH; Suh, PG; Oh, BH
- Date Issued
- 2002-03
- Publisher
- BLACKWELL MUNKSGAARD
- 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 Angstrom. The unit cell is likely to contain one molecule of SEDL, with a crystal volume per protein mass (V-M) of 2.36 Angstrom(3) Da(-1) and a solvent content of about 47.9% by volume. A native data set to 2.8 Angstrom resolution was obtained from a flash-cooled crystal using synchrotron radiation.
- Keywords
- LINKED SPONDYLOEPIPHYSEAL DYSPLASIA; TARDA; GENE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/19178
- DOI
- 10.1107/S0907444902001403
- ISSN
- 0907-4449
- Article Type
- Article
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, vol. 58, page. 564 - 566, 2002-03
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