Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.
- Resource Type
- Article
- Authors
- Wan, Qun; Kovalevsky, Andrey Y.; Wilson, Mark A.; Bennett, Brad C.; Langan, Paul; Dealwis, Chris
- Source
- Acta Crystallographica: Section F, Structural Biology Communications. Jun2014, Vol. 70 Issue 6, p814-818. 5p.
- Subject
- *X-ray diffraction
*ESCHERICHIA coli
*NEUTRON diffraction
*PROTON transfer reactions
*DIFFRACTOMETERS
- Language
- ISSN
- 2053-230X
A crystal of Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ of 4 × 1.3 × 0.7 mm (3.6 mm3) 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. [ABSTRACT FROM AUTHOR]