doi.bio/dorothee_liebschner


Dorothee Liebschner

Biography

Dorothee Liebschner is a computational research scientist in the field of biosciences. She currently works in the Molecular Biophysics and Integrated Bioimaging division of the Lawrence Berkeley National Laboratory. Liebschner's work focuses on macromolecular crystallography, neutron diffraction, and hydrogen atoms in crystallography.

Education and Career

Liebschner's educational background is unknown, but she has worked in various research areas. She has experience in molecular biophysics and integrated bioimaging, as well as macromolecular crystallography, neutron diffraction, and hydrogen atoms in crystallography.

Publications and Research

Liebschner has been a part of significant research projects and publications. One of her notable contributions was to an international team of scientists studying how plants split water during photosynthesis. This research involved capturing atomic-scale images of a protein complex found in plants, algae, and cyanobacteria using ultrafast X-ray lasers. The team's findings were published in Nature and provided insights into the mechanism of photosynthesis and the production of oxygen, protons, and electrons.

Awards and Recognition

Liebschner has received recognition for her contributions to the field of biosciences. She was among the honorees of the 2021 Berkeley Lab Director's Awards, which acknowledges the outstanding contributions of employees across all facets of laboratory activities.

Contact Information

Dorothee Liebschner can be contacted via her professional email address: dcliebschner@lbl.gov. Her phone number is (510) 486-5709, and her work address includes Building 33, Room 0345.

Conclusion

Dorothee Liebschner is a renowned computational research scientist who has made significant contributions to the field of biosciences. Her work in molecular biophysics and integrated bioimaging has advanced our understanding of complex biological processes such as photosynthesis. Liebschner's expertise in crystallography and diffraction techniques has contributed to important research publications and earned her recognition within the scientific community.

Dorothee Liebschner

Biography

Dorothee Liebschner is a computational research scientist in the field of biosciences. She works in the Molecular Biophysics and Integrated Bioimaging division and is based in Berkeley, as evidenced by her email address ending with "lbl.gov". Liebschner's work focuses on macromolecular crystallography, neutron diffraction, and hydrogen atoms in crystallography.

Publications

Liebschner has been part of an international team of scientists working on discovering how plants split water during photosynthesis. This research has led to groundbreaking, atomic-scale images of a protein complex found in plants, algae, and cyanobacteria. The images were captured using ultrafast X-ray lasers, and the findings were published in Nature.

Professional History

Liebschner has been associated with the Lawrence Berkeley National Laboratory, as indicated by her email address. She has also been recognised by the Biosciences Area Director's Awards for her outstanding contributions to lab activities.

Google Scholar

Dorothee Liebschner

Lawrence Berkeley National Laboratory

N/A

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix D Liebschner, PV Afonine, ML Baker, G Bunkóczi, VB Chen, TI Croll, … Acta Crystallographica Section D: Structural Biology 75 (10), 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:ULOm3_A8WrAC

Polder maps: improving OMIT maps by excluding bulk solvent D Liebschner, PV Afonine, NW Moriarty, BK Poon, OV Sobolev, … Acta Crystallographica Section D: Structural Biology 73 (2), 148-157, 2017 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:Tyk-4Ss8FVUC

Structure of photosystem II and substrate binding at room temperature ID Young, M Ibrahim, R Chatterjee, S Gul, FD Fuller, S Koroidov, … Nature 540 (7633), 453-457, 2016 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:UebtZRa9Y70C

An improved experimental databank of transferable multipolar atom models–ELMAM2. Construction details and applications S Domagała, B Fournier, D Liebschner, B Guillot, C Jelsch Acta Crystallographica Section A: Foundations of Crystallography 68 (3), 337-351, 2012 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:W7OEmFMy1HYC

AlphaFold predictions are valuable hypotheses and accelerate but do not replace experimental structure determination TC Terwilliger, D Liebschner, TI Croll, CJ Williams, AJ McCoy, BK Poon, … Nature Methods 21 (1), 110-116, 2024 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:maZDTaKrznsC

On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin D Liebschner, M Dauter, A Brzuszkiewicz, Z Dauter Acta Crystallographica Section D: Biological Crystallography 69 (8), 1447-1462, 2013 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:UeHWp8X0CEIC

Elucidation of the phosphate binding mode of DING proteins revealed by subangstrom X-ray crystallography D Liebschner, M Elias, S Moniot, B Fournier, K Scott, C Jelsch, B Guillot, … Journal of the American Chemical Society 131 (22), 7879-7886, 2009 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:LkGwnXOMwfcC

Announcing mandatory submission of PDBx/mmCIF format files for crystallographic depositions to the Protein Data Bank (PDB) PD Adams, PV Afonine, K Baskaran, HM Berman, J Berrisford, G Bricogne, … Acta Crystallographica Section D: Structural Biology 75 (4), 451-454, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:KlAtU1dfN6UC

On the influence of crystal size and wavelength on native SAD phasing D Liebschner, Y Yamada, N Matsugaki, M Senda, T Senda Acta Crystallographica Section D: Structural Biology 72 (6), 728-741, 2016 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:qjMakFHDy7sC

Hydrogen atoms in protein structures: high-resolution X-ray diffraction structure of the DFPase M Elias, D Liebschner, J Koepke, C Lecomte, B Guillot, C Jelsch, … BMC research notes 6, 1-7, 2013 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:ufrVoPGSRksC

Topological analysis of hydrogen bonds and weak interactions in protein helices via transferred experimental charge density parameters D Liebschner, C Jelsch, E Espinosa, C Lecomte, E Chabriere, B Guillot The Journal of Physical Chemistry A 115 (45), 12895-12904, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:9yKSN-GCB0IC

Accelerating crystal structure determination with iterative AlphaFold prediction TC Terwilliger, PV Afonine, D Liebschner, TI Croll, AJ McCoy, RD Oeffner, … Acta Crystallographica Section D: Structural Biology 79 (3), 234-244, 2023 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:r0BpntZqJG4C

Radiation decay of thaumatin crystals at three X-ray energies D Liebschner, G Rosenbaum, M Dauter, Z Dauter Acta Crystallographica Section D: Biological Crystallography 71 (4), 772-778, 2015 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:roLk4NBRz8UC

The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors M Sato, D Liebschner, Y Yamada, N Matsugaki, T Arakawa, SS Wills, … Journal of Biological Chemistry 292 (29), 12126-12138, 2017 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:WF5omc3nYNoC

Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition D Liebschner, PV Afonine, NW Moriarty, P Langan, PD Adams Acta Crystallographica Section D: Structural Biology 74 (8), 800-813, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:MXK_kJrjxJIC

Interactive comparison and remediation of collections of macromolecular structures NW Moriarty, D Liebschner, HE Klei, N Echols, PV Afonine, JJ Headd, … Protein Science 27 (1), 182-194, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:YsMSGLbcyi4C

CERES: a cryo-EM re-refinement system for continuous improvement of deposited models D Liebschner, PV Afonine, NW Moriarty, BK Poon, VB Chen, PD Adams Biological Crystallography 77 (1), 48-61, 2021 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:hC7cP41nSMkC

Implementation of the riding hydrogen model in CCTBX to support the next generation of X-ray and neutron joint refinement in Phenix D Liebschner, PV Afonine, AG Urzhumtsev, PD Adams Methods in enzymology 634, 177-199, 2020 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:9ZlFYXVOiuMC

Crystallographic analysis of murine p24γ2 Golgi dynamics domain M Nagae, D Liebschner, Y Yamada, K Morita‐Matsumoto, N Matsugaki, … Proteins: Structure, Function, and Bioinformatics 85 (4), 764-770, 2017 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:Y0pCki6q_DkC

Using predicted models in Phenix D Liebschner Acta Cryst 75, 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=SfjtO7wAAAAJ&citationforview=SfjtO7wAAAAJ:bEWYMUwI8FkC