MICROSTAR HF MICROFOCUS ROTATING ANODE

University of Salzburg

Salzburg | Website

Large equipment

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

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

Chemical and Structural Biology

Prof. Dr. Hans Brandstetter
Fachbereich Biowissenschaften, Schwerpunkt ACBN
0043 662 8044 7270
hans.brandstetter@sbg.ac.at
http://www.uni-salzburg.at/index.php?id=77&MP=77-44794
Please contact us via science.plus@sbg.ac.at, or contact the responsible person for this section, mentioned in the contact field
Department of chemistry & physics of materials, University of Salzburg
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
International PhD Program "Immunity in Cancer and Allergy"
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
Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity
2015
Freier R., Dall E., Brandstetter H.
Scientific Reports
http://www.nature.com/articles/srep12707
DOI: 10.1038/srep12707

Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.
2015
Dall E., Fegg J.C., 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 M.J., 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