Structural molecular biology in the Montoya Group

The Montoya Group works to illuminate the molecular details of cellular processes. This knowledge is the basis for the understanding of diseases and the possible development of treatments.


Research focus

The Montoya Group works in the interface between biology, physics and chemistry and uses molecular biology, X-ray crystallography and cryo-electron microscopy to dissect the working mechanisms of the macromolecules that constitute the cell’s machinery. Although these machines underlie all biological processes, there is a lack of knowledge of their function at the atomic level.

“Our approach is to use advanced methodology to understand basic cellular mechanisms at an atomic level. We investigate the structural details and function of macromolecules involved in cell cycle progression and genome integrity. Deciphering the working mechanisms of these important processes provides the basis for understanding disease.” says Guillermo Montoya

A recent leap in methodological development has overcome some of the barriers that avoided the study of large macromolecular complexes and allows for a degree of accuracy that has not been possible before. The Montoya group is part of this revolution and since 2017 the group has contributed to set up a state-of-the-art cryo-electron microscopy system that have accelerated their research.

Main findings

The CRISPR-Cas Cas12a/Cpf1 endonuclease is emerging as a powerful genome-editing tool. The group’s analysis of the Cpf1 structure gives important information about its DNA targeting mechanism.
Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage - Stella et al., Nature 2017
"Conformational Activation Promotes CRISPR-Cas12a Catalysis and Resetting of the Endonuclease Activity - Stella et al ., Cell 2018"

Visualizing phosphodiester-bond hydrolysis by an endonuclease” 
Molina et al., Nature Structural & Molecular Biology, 2015
The Montoya Group has described the first-of-its-kind catalytic mechanism of a homing endonuclease, I-DmoI, as it is cleaving its target DNA.

XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation
Mortuza et al., Nature Communications, 2014
By dissecting the mechanism by which XTACC3 and XMAP215 interacts, the group showed how microtubule elongation and spindle assembly during mitosis is promoted.

Staff of the Montoya Group

Group Leader: Professor and Research Director Guillermo Montoya

Staff of the Mann Group
Top row from the left: Rafael Molina, Vykintas Jauniskis, Stefano Stella, Pablo Mesa, Nicholas Sofos
Middle row: Emilija Ruksenaite, Melanie Weisser, Kamila Kamuda (former) , Diana Kowalik, Guillermo Montoya, Bhargav Saligram Prabhakar
Bottom row: Bijoya Paul, Claudia Weidling (former), Danyang Wang, Elisabeth Bragado Nilsson