Jose A. Gavira

TL;DR: A variety of approaches have been developed that combine the spectrum of factors that effect and promote crystallization, and among the most widely used are vapor diffusion, dialysis, batch and liquid-liquid diffusion.

TL;DR: Results support the notions that Precambrian life was thermophilic and that proteins can evolve from substrate-promiscuous generalists into specialists during the course of natural evolution and highlight the biotechnological potential of laboratory resurrection of Precambrians proteins.

TL;DR: The implementation of this technique linked to the advancement of current crystallography software leads to a powerful structure determination method consolidating crystal growth, X-ray data collection, and ab initio phase determination into one without crystal manipulation.

TL;DR: This work investigates the differences in conformational dynamics of the ancient and extant β-lactamases through MD simulations and quantifies the contribution of each position to functionally related dynamics through Dynamic Flexibility Index, leading to testable predictions.

TL;DR: X-ray crystal structures of seven laboratory resurrections of Precambrian thioredoxins dating up to approximately four billion years ago show a remarkable degree of structure conservation, which supports a punctuated-equilibrium model of structure evolution in which the generation of new folds occurs over comparatively short periods and is followed by long periods of structural stasis.