D
Daniela Stock
Researcher at University of New South Wales
Publications - 42
Citations - 8494
Daniela Stock is an academic researcher from University of New South Wales. The author has contributed to research in topics: ATP synthase & ATP synthase gamma subunit. The author has an hindex of 28, co-authored 42 publications receiving 8168 citations. Previous affiliations of Daniela Stock include Free University of Berlin & Max Planck Society.
Papers
More filters
Journal ArticleDOI
Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA.
TL;DR: The crystal structure of reverse gyrase from Archaeoglobus fulgidus is determined in the presence and absence of nucleotide cofactor, providing the first view of an intact supercoiling enzyme and suggesting a model for how the two domains of the protein cooperate to positively supercoil DNA.
Journal ArticleDOI
Robotic nanolitre protein crystallisation at the MRC Laboratory of Molecular Biology.
TL;DR: High-throughput robotic systems to screen and optimise crystallisation conditions of biological macromolecules with the aim of making difficult structural biology projects easier are set up.
Journal ArticleDOI
The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase
Lawrence K. Lee,Alastair G. Stewart,Mhairi Donohoe,Ricardo A. Bernal,Daniela Stock,Daniela Stock +5 more
TL;DR: The crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus, which contains a heterodimeric right-handed coiled coil, a protein fold never observed before, is determined and fitted into the 23 Å resolution EM density of the intact A-ATPase complex.
Journal ArticleDOI
Ion mobility–mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility
Min Zhou,Argyris Politis,Argyris Politis,Roberta B. Davies,Idlir Liko,Kuan Jung Wu,Alastair G. Stewart,Alastair G. Stewart,Daniela Stock,Daniela Stock,Carol V. Robinson +10 more
TL;DR: Differences that can be related to conformational changes in the Vo complex triggered by ATP binding are revealed by isolating complexes at different phases of cell growth and manipulating nucleotides, metal ions and pH during isolation.
Journal ArticleDOI
Three-Dimensional Structure of the Intact Thermus thermophilus H+-ATPase/Synthase by Electron Microscopy
Ricardo A. Bernal,Daniela Stock +1 more
TL;DR: A three-dimensional reconstruction of the intact H+-ATPase/synthase from Thermus thermophilus has revealed the presence of two interconnected peripheral stalks, a well-defined central stalk, and a hexagonally shaped hydrophobic domain.