Crystallization and preliminary crystallographic analysis of the fourth FAS1 domain of human BigH3

Ji Ho Yoo, Eung Kweon Kim, Jongsun Kim, Hyun Soo Cho

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The protein BigH3 is a cell-adhesion molecule induced by transforming growth factor-β (TGF-β). It consists of four homologous repeat domains known as FAS1 domains; mutations in these domains have been linked to corneal dystrophy. The fourth FAS1 domain was expressed in Escherichia coli B834 (DE3) (a methionine auxotroph) and purified by DEAE anion-exchange and gel-filtration chromatography. The FAS1 domain was crystallized using the vapour-diffusion method. A SAD diffraction data set was collected to a resolution of 2.5 Å at 100 K. The crystal belonged to space group P61 or P65 and had two molecules per asymmetric unit, with unit-cell parameters a = b = 62.93, c = 143.27 Å, α = β = 90.0, γ = 120.0°.

Original languageEnglish
Pages (from-to)893-895
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number10
DOIs
Publication statusPublished - 2007 Sep 19

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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