Abstract

X-ray crystallography has long been a key method in solving the three-dimensional structure of proteins. Structural information is essential for unraveling the molecular function of proteins and structure-based drug design. However, there are several obstacles associated with the structural determination of proteins using X-ray crystallography, such as the generation of a large amount of protein samples, instability of purified proteins, and difficulty in obtaining large and well-diffracting crystals, all of which can prolong the process of determining the crystal structure, from months to years. Over the past decade, new techniques and strategies have been developed to assist X-ray crystallographers in overcoming some of these obstacles. In this chapter, we discuss some of these technological advances. Familiarity with these new developments would benefit researchers in both academic and industrial environments who study macromolecular structural dynamics using X-ray crystallography.

Original languageEnglish
Title of host publicationAdvanced Spectroscopic Methods to Study Biomolecular Structure and Dynamics
PublisherElsevier
Pages309-355
Number of pages47
ISBN (Electronic)9780323991278
ISBN (Print)9780323993661
DOIs
StatePublished - Jan 1 2022

Keywords

  • Crystallization chaperones
  • In situ X-ray screening
  • Membrane proteins
  • Microcrystal electron diffraction
  • Neutron macromolecular crystallography
  • On-chip crystal growth
  • Serial femtosecond crystallography
  • Size exclusion chromatography with multiangle light scattering
  • X-ray crystallography
  • X-ray free-electron lasers

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