The measurements at SACLA are based on serial femtosecond crystal structure analysis which continuously measures one diffraction image from one microcrystal which is destroyed during measurmenet. With two proteins, modified at one single methionine residue by seleno-methionine, highly accurate data were acquired from as little as 30,000 or 60,000 micrometer size microcrystals, respectively, and 3D structures at resolution were obtained (measurement time about 1 hour). This new method makes prior formation of large crystals unnecessary and is hoped to contribute to the structure elucidation of proteins such as membrane bound receptors which are difficult to be crystallized.
RIKEN news release, August 23, 2017
SACLA’s X-ray free electron laser (XFEL) solves 3D structures of 2 seleno-methionine tagged proteins from microcrystals