Good news, everyone!
"If you want to map the tiniest parts of a protein, you only have a few options: You can coax millions of individual protein molecules to align into crystals and analyze them using x-ray crystallography. Or you can flash-freeze copies of the protein and bombard them with electrons, a lower resolution method called cryo–electron microscopy (cryo-EM). Now, for the first time, scientists have sharpened cryo-EM's resolution to the atomic level, allowing them to pinpoint the positions of individual atoms in a variety of proteins at a resolution that rivals x-ray crystallography's.
"This is just amazing," says Melanie Ohi, a cryo-EM expert at the University of Michigan, Ann Arbor. "To see this level of detail, it's just beautiful." Because the heightened resolution reveals exactly how complex cellular machines carry out their jobs, improvements in cryo-EM should yield countless new insights into biology."
"If you want to map the tiniest parts of a protein, you only have a few options: You can coax millions of individual protein molecules to align into crystals and analyze them using x-ray crystallography. Or you can flash-freeze copies of the protein and bombard them with electrons, a lower resolution method called cryo–electron microscopy (cryo-EM). Now, for the first time, scientists have sharpened cryo-EM's resolution to the atomic level, allowing them to pinpoint the positions of individual atoms in a variety of proteins at a resolution that rivals x-ray crystallography's.
"This is just amazing," says Melanie Ohi, a cryo-EM expert at the University of Michigan, Ann Arbor. "To see this level of detail, it's just beautiful." Because the heightened resolution reveals exactly how complex cellular machines carry out their jobs, improvements in cryo-EM should yield countless new insights into biology."