Gunnar I. Berglund

TL;DR: An effective strategy to obtain crystal structures for high-valency redox intermediates is described and a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP) is presented.

TL;DR: In this paper, the X-ray structure of human trypsin IV in complex with the inhibitor benzamidine at 1.7 A resolution was reported, revealing the orientation of the side-chain of Arg193, which occupies an extended conformation and fills the S2′ subsite.

TL;DR: Comparisons with structures obtained as part of “time-resolved” studies on the reacting acyl-enzyme complex at >pH 7 indicate small but significant structural differences, consistent with the proposed synchronization of ester hydrolysis and substrate release.

TL;DR: The H. grisea enzyme was much more stable to irreversible thermal denaturation than the Trichoderma reesei enzyme, and the three cysteines in H.grisea Cel12A play an important role in the thermal stability of this protein, although they are not involved in a disulfide bond.

TL;DR: X‐ray structures of the chitinase catalytic domain from wild‐type (apo, as well as with chloride ions bound) and a Glu234Ala mutant enzyme are reported, solved by molecular replacement and refined at 1.53, 1.8 and 1.7 Å resolution, respectively.