Crystallography of large biological macromolecules can be achieved while maintaining their solution state. The best known example is the ribosome.
Today, liquid nitrogen cryo cooling is used for protein crystallography at every synchrotron around the world. Radiation damaged is reduced by more than 70 fold at cryo temperatures. A recent review paper explains the development of reduced radiation damage in macromolecular crystals at Synchrotrons and describes how more than 90% of all structures deposited in the Protein Data Bank used cryo cooling in their determination.
2020 Haas, DJ. The early history of cryo-cooling for macromolecular crystallography (2020)
	IUCrJ (2020). 7, 148–157.  https://journals.iucr.org/m/issues/2020/02/00/be5283/be5283.pdf
1970 Haas, D.J., and Rossmann, M.G.
             Crystallographic Studies on Lactate Dehydrogenase at -75 C.  Acta Crystallogr.  (1970), B26, 998.