The aim of structural biology has been always the study of biological macromolecules structures and their mechanistic behaviour at molecular level. To achieve its goal, multiple biophysical methods and approaches have become part of the structural biology toolbox. Considered as one of the pillars of structural biology, X-ray crystallography has been the most successful method for solving three-dimensional protein structures at atomic level to date. It is however limited by the success in obtaining well-ordered protein crystals that diffract at high resolution. This is especially true for challenging targets such as membrane proteins (MPs). Understanding structure-function relationships of MPs at the biochemical level is vital for medicine and drug discovery as they play critical roles in many cellular processes. Though difficult, structure determination of MPs by X-ray crystallography has significantly improved in the last two decades, mainly due to many relevant technological and methodological developments. Today, numerous MP crystal structures have been solved, revealing many of their mechanisms of action. Yet the field of structural biology has also been through significant technological breakthroughs in recent years, particularly in the fields of single particle electron microscopy (cryo-EM) and X-ray free electron lasers (XFELs). Here we summarise the most important advancements in the field of MP crystallography and the significance of these developments in the present era of modern structural biology.
-
Cover Image
Cover Image
The plasma membrane of lymphocytes is highly compartmentalized in so-called nanodomains or protein islands. Proteins such as Caveolin-1 (pink), tetraspanins (blue) or flotillins (violet) define these protein islands and thereby regulate the functioning of the immune system. In this issue (see pages 2387–2397), Schaffer and Minguet discuss the importance of these protein islands regarding lymphocyte activation and the development of immunopathologies. This cover artwork has been created by Susana Minguet.
Membrane protein crystallography in the era of modern structural biology
Tristan O. C. Kwan, Danny Axford, Isabel Moraes; Membrane protein crystallography in the era of modern structural biology. Biochem Soc Trans 18 December 2020; 48 (6): 2505–2524. doi: https://doi.org/10.1042/BST20200066
Download citation file:
Sign in
Sign in to your personal account
Captcha Validation Error. Please try again.