Daniela Stock

TL;DR: A 2.25-Å resolution crystal structure of the peripheral stalk from Thermus thermophilus A-type ATPase/synthase is presented and bending and twisting motions inherent within the structure are identified that accommodate and complement a radial wobbling of the ATPase headgroup as it progresses through its catalytic cycles, while still retaining azimuthal stiffness necessary to counteract rotation of the central stalk.

TL;DR: The factor for inversion stimulation (FIS) binds as a homodimeric molecule to a loose 15 nucleotide consensus sequence in DNA, which stimulates DNA-related processes, such as DNA inversion and excision, it activates transcription of tRNA and rRNA genes and it regulates its own synthesis.

TL;DR: The crystal structure of subunit F of vacuole‐type ATPase/synthase (prokaryotic V‐ATPase) reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY.

TL;DR: This is the first description of phage display-derived antibody selection against a multi-subunit membrane protein used for purification and single particle analysis by electron microscopy and the first instance of the derivation of subunit stoichiometry by tandem mass spectrometry to an intact membrane protein complex.

TL;DR: It is demonstrated that Escherichia coli FliG, one of the earliest-assembling flagellar motor proteins, forms ordered ring structures via domain-swap polymerization, which in other proteins has been associated with uncontrolled and deleterious protein aggregation.