Après la Révolution : où la cristallographie aux rayons X se situe dans le contexte de la cryomicroscopie électronique
DOI :
https://doi.org/10.18192/osurj.v5i1.8046Résumé
Malgré l’essor de la cryomicroscopie électronique (cryo-ME) comme méthode de premier plan pour la détermination des structures ces dernières années après sa « révolution de la résolution », la cristallographie aux rayons X continue de jouer un rôle clé et crucial dans le domaine de la biologie structurale. Bien que la cryo-ME permette de résoudre des macromolécules non cristallisables, la cristallographie aux rayons X reste plus efficace pour atteindre la résolution atomique et a la capacité de définir les orientations et interactions des chaînes latérales et des ligands, ce qui la rend utile dans l’étude mécanistique et enzymologique des protéines. Cette revue met en lumière la cristallographie aux rayons X et souligne que la cristallographie aux rayons X et la cryo-ME restent des méthodes complémentaires pour déterminer les structures macromoléculaires, au lieu que la première soit entièrement remplacée par la seconde. Dans ce contexte, avec d’autres méthodes d’analyse structurale, la cristallographie aux rayons X s’est révélée s’adapter au paysage évolutif de la biologie structurale.
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