Kathrin Meindl

TL;DR: ARCIMBOLDO combines the location of small fragments with Phaser and density modification with SHELXE of all possible Phaser solutions.

TL;DR: A mechanism for oligomerization of Lsr2 via protease-activation leading to chromosome compaction and protection, and concomitant down-regulation of large numbers of genes is suggested.

TL;DR: A functional role for this enzyme is proposed as befits the uniqueness of its two-domain structure as well as the structural and catalytic properties of MltC, one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli.

TL;DR: The crystal structure of the first endolytic peptidoglycan lytic transglycosylase MltE from Escherichia coli is reported here and reveals how the enzyme is sequestered on the inner leaflet of the outer membrane.

TL;DR: The structure solution of DNA-binding protein structures and complexes based on the combination of location of DNA -binding protein motif fragments with density modification in a multi-solution frame is described.