University of Salzburg
Salzburg | Website
Short Description
The x-ray diffractometer consists of an x-ray generator, x-ray optics (mirror system), a Cryo system and an x-ray area counter. The x-ray generator produces x-ray radiation by means of a copper rotary anode (Cu Kα , 1.54 Å), which is further focused and monochromatized through a mirror system.
The nitrogen powered Cryo system allows a temperature control in the temperature window from 80 to 300 kelvin to a degree. The imaging plate technology of the x-ray detector allows a detection of x-ray diffraction with extremely long cell axes of up to 500 Å and a resolution of better than 1.5 Å.
Contact Person
Univ-Prof. Dr. Hans Brandstetter
Research Services
X-ray structure analysis of macromolecules (mainly proteins and DNA)
Methods & Expertise for Research Infrastructure
The X-ray diffractometer is the instrumental centerpiece for the molecular structure elucidation. The present device is designed especially for the elucidation of biologically relevant macromolecules such as proteins and DNA. The structure elucidation is the key for the mechanistic understanding of these molecules. Specific applications include proteins with relevance in the fields of immunology, allergy, antigen processing, pathogen-host interaction, blood clotting and others. All these examined proteins play a significant role in health related topics. The structure determinations achieved in this way have already opened up new possibilities for development in the diagnosis and therapy of the respective disease areas.
Allocation to Core Facility
University of Innsbruck
Medical University of Vienna
Technical University of Munich
University of Antwerp
Shire Bioscience Vienna
Novo Nordisk Copenhagen
Universidade de Lisboa
University of Massachusetts, Amherst
MPI Golm
Sanford-Burnham Institute La Jolla
University of Bielefeld
University of Cologne
Helmholtz Research Centre Jülich
Emory University, Medical School (USA)
MPI Martinsried
SALK, PMU
DKFZ Heidelberg
Lund University (Sweden)
Universidade Federal de Minas Gerais
2009-2021
Huber Christian; Aberger Fritz, Brandstetter Johann, Duschl Albert, Ferreira Fatima, Gratz Iris, Greil Richard, Hartmann Tanja, Risch Angela, Wessler Silja
FWF
http://ica.sbg.ac.at
Kofaktor- und Substratabhängige Aktivierung des Gerinnungsfaktors IXa
01.07.2011-30.6.2014
Brandstetter Johann
FWF
Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars
01.10.2013-30.09.2018
Huber christian (Sprecher); Brandstetter Johann, Cabrele Chiara, Gadermaier Gabriele, Stutz Hanno
CD Forschungsgesellschaft, Sandoz, Thermo Fisher Scientific, bmWFJ
Funktionelle Prinzipien der Legumain-Macrocypin Interaktion
2019-2022
Elfriede Dall
FWF
Mechanismus des bakteriellen Kollagenabbaus
2019-2022
Esther Schönauer
FWF
2022
T Elamin, NP Santos, P Briza, H Brandstetter, E Dall
Journal of Biological Chemistry 298 (10)
https://doi.org/10.1016/j.jbc.2022.102502
Discovery and Characterization of Synthesized and FDA-Approved Inhibitors of Clostridial and Bacillary Collagenases
2022
A Alhayek, AS Abdelsamie, E Schönauer, V Camberlein, E Hutterer, ..., H Brandstetter, A Hirsch
Journal of Medicinal Chemistry 65 (19), 12933-12955
https://doi.org/10.1021/acs.jmedchem.2c00785
Dichlorophenylpyridine-based molecules Inhibit furin through an induced-Fit mechanism
2022
SO Dahms, G Schnapp, M Winter, FH Büttner, M Schlepütz, C Gnamm, … & H Brandstetter
ACS chemical biology 17 (4), 816-821
https://doi.org/10.1021/acschembio.2c00103
The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities
2021
Elfriede Dall, Vesna Stanojlovic, Fatih Demir, Peter Briza, Sven O Dahms, Pitter F Huesgen, Chiara Cabrele, Hans Brandstetter
ACS catalysis
https://doi.org/10.1021/acscatal.1c02057
Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.
2015
Dall E, Fegg JC, Briza P, Brandstetter H.
Angwandte Chemie
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4506564/
DOI: 10.1002/anie.201409135
Posttranslational modifications of intact proteins detected by NMR spectroscopy: application to glycosylation.
2015
Schubert M, Walczak MJ, Aebi M, Wider G.
Angewandte Chemie
http://onlinelibrary.wiley.com/wol1/doi/10.1002/anie.201502093/abstract
DOI: 10.1002/anie.201502093
Stabilization of the Dimeric Birch Pollen Allergen Bet v 1 Impacts Its Immunological Properties
2014
Kofler S, Ackaert C, Samonig M, Asam C, Briza P, Horejs-Hoeck J, Cabrele C, Ferreira F, Duschl A, Huber C, Brandstetter H.
The Journal of Biological Chemistry
http://www.jbc.org/content/289/1/540.long
DOI: 10.1074/jbc.M113.518795
Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
2013
Dall E, Brandstetter H.
PNAS
http://www.pnas.org/content/110/27/10940.long
DOI: 10.1073/pnas.1300686110
Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.
2011
Eckhard U, Schönauer E, Nüss D, Brandstetter H.
Nature Structural and Molecular Biology
http://www.nature.com/nsmb/journal/v18/n10/full/nsmb.2127.html
DOI: 10.1038/nsmb.2127
Molecular metamorphosis in polcalcin allergens by EF-hand rearrangements and domain swapping
2010
Magler I, Nüss D, Hauser M, Ferreira F, Brandstetter H.
The FEBS Journal
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2010.07671.x/abstract
DOI: 10.1111/j.1742-4658.2010.07671.x
Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen
2016
Machado Y., Freier R., Scheiblhofer S., Thalhamer T., Mayr M., Briza P., Grutsch S., Ahammer L., Fuchs J.E., Wallnoefer H.G., Isakovic A., Kohlbauer V., Hinterholzer A., Steiner M., Danzer M., Horejs-Hoeck J., Ferreira F., Liedl K.R., Tollinger M., Lackner P., Johnson C.M., Brandstetter H., Thalhamer J. and Weiss R.
J Allergy Clin Immunol
http://www.sciencedirect.com/science/article/pii/S0091674915013664
10.1016/j.jaci.2015.09.026