Abstract
Neutron diffraction is uniquely sensitive to hydrogen positions and protonation state. In that context structural information from neutron data is complementary to that provided through X-ray diffraction. However, there are practical obstacles to overcome in fully exploiting the potential of neutron diffraction, i.e. low flux and weak scattering. Several approaches are available to overcome these obstacles and we have investigated the simplest: increasing the diffracting volume of the crystals. Volume is a quantifiable metric that is well suited for experimental design and optimization techniques. By using response surface methods we have optimized the xylose isomerase crystal volume, enabling neutron diffraction while we determined the crystallization parameters with a minimum of experiments. Our results suggest a systematic means of enabling neutron diffraction studies for a larger number of samples that require information on hydrogen position and/or protonation state.
| Original language | English |
|---|---|
| Pages (from-to) | 621-632 |
| Number of pages | 12 |
| Journal | European Biophysics Journal |
| Volume | 35 |
| Issue number | 7 |
| DOIs | |
| State | Published - Sep 2006 |
Funding
Acknowledgments We would like to thank Genencor International for the generous donation of the xylose isomerase used in this study, Riccardo Leardi for initial discussions on experiment design and Richard Kephart for assistance in the initial stages. MvdW and MD are contractors to NASA through BAE Systems Analytical Solutions. This work was supported through NASA grant NAG8-1916 and the Oishei Foundation.