Overexpression, crystallization and preliminary X-ray crystallographic analysis of dihydrofolate reductase from bacteriophage T4

Yun Kyung Oh, Jinho Moon, Jae Young Lee, Sangwoo Cho, Whanchul Shin, Se Won Suh

Research output: Contribution to journalArticle


Dihydrofolate reductase (DHFR) from bacteriophage T4 is a homodimer consisting of 193-residue subunits. It has been crystallized in the presence of the cofactor (NADPH) and an inhibitor (aminopterin) at 296 K using sodium chloride as precipitant. The crystals are tetragonal, belonging to the space group P4122 (or P4322), with unit-cell parameters a = b = 61.14, c = 123.23 Å under cryogenic conditions. The asymmetric unit contains a single subunit, with a corresponding V(m) of 2.65 Å3 Da-1 and a solvent content of 53.6%. Native data have been collected from a crystal to 1.9 Å resolution using synchrotron X-rays.

Original languageEnglish (US)
Pages (from-to)775-777
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Issue number6
Publication statusPublished - 2000
Externally publishedYes


ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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