Small-angle scattering makes it possible to solve structural biology problems without specific sample preparation, which is typical for methods such as X-ray diffraction of protein crystals or cryo-electron microscopy of proteins. In our review, it is shown how to use small-angle scattering to address biological problems. The use of small-angle scattering is suggested for applications as a tool to control the quality of the assembly of proteins and protein complexes and to test the identity of the structural organization of biological objects in the native state and in prepared samples before measurements by X-ray diffraction or cryo-electron microscopy. This work demonstrates the possibilities of the small-angle neutron scattering spectrometer YuMO based on the IBR-2 pulsed reactor (Laboratory of neutron physics, Joint Institute for Nuclear Research, Dubna, Russia) to solve a whole array of problems, with an eye toward applying these in biophysics, structural biology, and biotechnology. This review presents and discusses the main findings of the studies of various biological systems obtained by using the setup small-angle scattering of neutrons YuMO. The possibilities of development of structural biology methods with the help of small-angle scattering, including protein crystallization, are shown.
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