摘要
Protein microcrystals magnetically aligned in D2O hydrogels were subjected to neutron diffraction measurements, and reflections were observed for the first time to a resolution of 3.4 angstrom from lysozyme microcrystals (similar to 10 x 10 x 50 mu m). This result demonstrated the possibility that magnetically oriented microcrystals consolidated in D2O gels may provide a promising means to obtain single-crystal neutron diffraction from proteins that do not crystallize at the sizes required for neutron diffraction structure determination. In addition, lysozyme microcrystals aligned in H2O hydrogels allowed structure determination at a resolution of 1.76 angstrom at room temperature by X-ray diffraction. The use of gels has advantages since the microcrystals are measured under hydrated conditions.
- 出版日期2016-7