On the cover: single surface substitutions improve the crystallizability and diffraction properties of a flexible two-domain protein, even if they increase the entropy of the respective residue. Read more at
doi.org/10.1107/S205...
On the cover: single surface substitutions improve the crystallizability and diffraction properties of a flexible two-domain protein, even if they increase the entropy of the respective residue. Read more at
doi.org/10.1107/S205...
On the cover: two different orientations of the NAD coenzyme are fortuitously observed in the NAD+-bound structure of a short-chain dehydrogenase from Brucella ovis. Find out more at doi.org/10.1107/S205...
On the cover: two different orientations of the NAD coenzyme are fortuitously observed in the NAD+-bound structure of a short-chain dehydrogenase from Brucella ovis. Find out more at doi.org/10.1107/S205...
The cover shows the crystal structure of Cryptococcus humicola D-aspartate oxidase, which has a unique homotetrameric architecture in contrast to other known D-amino-acid oxidases. Read more at doi.org/10.1107/S205...
The cover shows the crystal structure of Cryptococcus humicola D-aspartate oxidase, which has a unique homotetrameric architecture in contrast to other known D-amino-acid oxidases. Read more at doi.org/10.1107/S205...