文摘
Neutron crystallography is an experimental method for visualizing the hydrogen atoms of proteins, thereby elucidating the mechanism of the target proteins. The technique requires large crystals of proteins to overcome the low flux of the available neutron beam. We previously reported that top-seeded solution growth (TSSG) is an efficient strategy for rapidly growing large protein crystals, but obstacles still remain. Here we report a syringe-type TSSG for growing protein crystals. In this method, a seed crystal is hung in the syringe. The method permits small protein crystals to be attached with the desired crystal orientation under an optical microscope. Similarly to previous results of TSSG, the shape of the lysozyme and superoxide dismutase crystals were strongly influenced by the orientation of the seed crystal. This new approach is expected to expand the scope of target proteins for neutron crystallographic analysis.