
Pedro Dinis, TCSM Postdoctoral Reseacher, Department of Biochemistry
Given free-reign by the Turku Collegium of Science and Medicine to write about anything made the choice of topic quite easy, as macromolecular crystallography has accompanied my budding scientific career. It also comes at a critical juncture in the field with the emergence of cryogenic electronic microscopy (Cryo-EM).
Two parts science, one part art
A young researcher eagerly enters a lab for the first time. His goal a simple affair, to crystallize a protein. He manages to get his protein both as pure and as concentrated as possible. The future is looking bright. But, what is the next step?
One could scour the literature regarding the topic of protein crystallization, without finding the precise way to do so. And the reason is not some cabal of old scientists gate-keeping future generations, but a simpler explanation: there is no exact way to lead a protein to form crystals. Each protein is as each individual, a unique, special snowflake. All that researcher has, as indeed we all do, are simple guidelines. You need to mix the protein with SOMETHING that will lead it to a controlled precipitation, i.e. crystal formation, instead of uncontrolled precipitation (think of curdling milk). Because the Universe is vast and full of SOMETHINGs, the best the scientific community has to offer is mixtures of salts, buffers and other precipitants that were previously shown to crystallize a protein (crystallization screens). Continue reading







