Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex

Maria A. Schumacher, Kang Yell Choi, Howard Zalkin, Richard G. Brennan

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The purine repressor (PurR) is a DNA-binding protein, which together with a purine corepressor serves to regulate de novo purine and pyrimidine biosynthesis in Escherichia coli. PurR belongs to the structurally homologous lac repressor family of transcription regulators. A PurR-hypoxanthine-DNA complex has been crystallized, with DNA encompassing the high affinity purF operator site and which is 16 base-pairs long with 5’-deoxynucleoside overhangs on each complementary strand. The crystals diffract to better than 2.6 AÅ and take the orthorhombic space group C2221, with unit cell dimensions a = 175.9 AÅ, b = 94.8 AÅ and c = 81.8 AÅ. The structure determination of this PurR-hypoxanthine-DNA complex will provide the first high resolution view of a LacI member-DNA complex.

Original languageEnglish
Pages (from-to)302-305
Number of pages4
JournalJournal of Molecular Biology
Volume242
Issue number3
DOIs
Publication statusPublished - 1994 Sep 22

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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