Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+

Qun Wan, Andrey Y. Kovalevsky, Mark A. Wilson, Brad C. Bennett, Paul Langan, Chris Dealwis

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A crystal of Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ of 4 × 1.3 × 0.7 mm (3.6 mm 3) in size was obtained by sequential application of microseeding and macroseeding. A neutron diffraction data set was collected to 2.0 Å resolution using the IMAGINE diffractometer at the High Flux Isotope Reactor within Oak Ridge National Laboratory. A 1.6 Å resolution X-ray data set was also collected from a smaller crystal at room temperature. The neutron and X-ray data were used together for joint refinement of the ecDHFR-folate- NADP+ ternary-complex structure in order to examine the protonation state, protein dynamics and solvent structure of the complex, furthering understanding of the catalytic mechanism.

Original languageEnglish (US)
Pages (from-to)814-818
Number of pages5
JournalActa Crystallographica Section F:Structural Biology Communications
Issue number6
Publication statusPublished - Jun 2014



  • Escherichia coli
  • dihydrofolate reductase
  • protonation state

ASJC Scopus subject areas

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

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