J
Jonathan C. Brooks-Bartlett
Researcher at University of Oxford
Publications - 7
Citations - 297
Jonathan C. Brooks-Bartlett is an academic researcher from University of Oxford. The author has contributed to research in topics: Protein Data Bank & Absorbed dose. The author has an hindex of 5, co-authored 7 publications receiving 205 citations.
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Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
Mark D. White,Maria Klecker,Richard J. Hopkinson,Daan A. Weits,Carolin Mueller,Carolin Mueller,Christin Naumann,Rebecca O’Neill,James Wickens,Jiayu Yang,Jonathan C. Brooks-Bartlett,Elspeth F. Garman,Tom N. Grossmann,Tom N. Grossmann,Nico Dissmeyer,Emily Flashman +15 more
TL;DR: It is directly demonstrated that PCO dioxygenase activity produces Cys-sulfinic acid at the N terminus of an ERF-VII peptide, which then undergoes efficientArginylation by an arginyl transferase (ATE1) in plants, and a substrate of ATE1 in plants.
Journal ArticleDOI
Estimate your dose: RADDOSE-3D.
TL;DR: RADDOSE‐3D, a software tool allowing the estimation of the dose absorbed in a macromolecular crystallography diffraction experiment, is presented, giving a universal “x‐axis” against which to plot various metrics.
Journal ArticleDOI
Development of tools to automate quantitative analysis of radiation damage in SAXS experiments.
Jonathan C. Brooks-Bartlett,Rebecca A. Batters,Charles S. Bury,Edward D. Lowe,Helen M. Ginn,Adam Round,Adam Round,Elspeth F. Garman +7 more
TL;DR: Radiation damage analysis with experimental SAXS data allows for the quantitative comparison of the efficacy of various additive radioprotectant compounds.
Journal ArticleDOI
The Nobel Science: One Hundred Years of Crystallography
TL;DR: X-ray crystallography is the most common technique for the determination of three-dimensional crystalline structures at the atomic scale as discussed by the authors, and it has developed into an indispensable tool for material scientists and structural biologists worldwide.
Journal ArticleDOI
RABDAM: quantifying specific radiation damage in individual protein crystal structures
TL;DR: A program to measure the extent of specific radiation damage suffered by an individual protein crystal structure, suitable for running on any standard-format PDB or mmCIF file, is presented.