Short Description
The device consists of: 8-channel pipetting unit; Coil with 26,000 pipettes; Pipette loading unit; Calibration block; Guide block; Welding bracket for hanging drop applications; Computer; Control and evaluation software. The device allows reproducible pipetting steps in the volume range 25 nl to 1.2 µl with highly viscous liquids, a humidity chamber provides protection against evaporation of the nanoliter drops.
Contact Person
Univ.-Prof. Dr. Johann Brandstetter
Research Services
crystallisation campaigns
Methods & Expertise for Research Infrastructure
The crystallisation of a biomolecule represents a major challenge in the determination of its three-dimensional structure. The crystallisation robot enables the miniaturization of crystallisation campaigns to the nanolitre scale. This reduction enables an up to 100-fold reduction of the required protein, or conversely, a corresponding depth increase of the crystallization campaigns with identical protein usage. Importantly, this nanoliter robotics allow to carry out structural investigations on proteins, which can be produced at inherently low yield, e.g., membrane proteins. Finally, by its unique contamination-free working procedure the robot also qualifies for sensitive pipetting applications such as (epi) genomics.
Allocation to research infrastructure
SALK, PMU
Medizinische Universität Wien
Technische Universität München
Novo Nordisk Kopenhagen
Universität Köln
Helmholtz Forschungszentrum Jülich
Emory University, Medical School (USA)
MPI Martinsried
Universidade Federal de Minas Gerais, Brasilien
2023-2025
Elfriede Dall
FWF
International PhD Program "Immunity in Cancer and Allergy"
01.08.2008 - 31.12.2017
Thalhamer Josef (Projektleiter); Aberger Fritz, Brandstetter Johann, Duschl Albert, Ferreira Fatima, Gratz Iris, Greil Richard, Hartmann Tanja, Huber Christian, Risch Angela, Wessler Silja
FWF
http://www.uni-salzburg.at/index.php?id=86&MP=200731-200747
Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars
01.10.2013-30.06.2021
Huber christian (Sprecher); Brandstetter Johann, Cabrele Chiara, Gadermaier Gabriele, Stutz Hanno
CD Forschungsgesellschaft, Sandoz, Thermo Fisher Scientific, bmWFJ
http://cdl-biosimilars.sbg.ac.at/
Entwicklung konformationsspezifischer Furin-Inhibitoren
13.05.2020-12.05.2022
Sven Dahms, Hans Brandstetter
FWF
https://fwf.ac.at
2024
Roman W. Lange, Konstantin Bloch, Miriam Ruth Heindl, Jan Wollenhaupt, Manfred S. Weiss, Hans Brandstetter, Gerhard Klebe, Franco H. Falcone, Eva Böttcher-Friebertshäuser, Sven O. Dahms, Torsten Steinmetzer
ChemMedChem
https://doi.org/10.1002/cmdc.202400057
Inhibitors of the Elastase LasB for the Treatment of Pseudomonas aeruginosa Lung Infections
2023
Jelena Konstantinović, Andreas M. Kany, Alaa Alhayek, Ahmed S. Abdelsamie, Asfandyar Sikandar, Katrin Voos, Yiwen Yao, Anastasia Andreas, Roya Shafiei, Brigitta Loretz, Esther Schönauer, Robert Bals, Hans Brandstetter, Rolf W. Hartmann, Christian Ducho, Claus-Michael Lehr, Christoph Beisswenger, Rolf Müller, Katharina Rox, Jörg Haupenthal, and Anna K.H. Hirsch
ACS Central Science
https://doi.org/10.1021/acscentsci.3c01102
Structural and functional studies of legumain–mycocypin complexes revealed a competitive, exosite-regulated mode of interaction
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
Phosphonate as Stable Zinc‐binding Group for Inhibitors of Clostridial Collagenase H (ColH) as Pathoblocker Agents
2021
Katrin Voos, Esther Schönauer, Alaa Alhayek, Jörg Haupenthal, Anastasia Andreas, Rolf Müller, Rolf W Hartmann, Hans Brandstetter, Anna KH Hirsch, Christian Ducho
ChemMedChem
https://doi.org/10.1002/cmdc.202000994
https://doi.org/10.1002/cmdc.202000994
The Basicity Makes the Difference: Improved Canavanine-Derived Inhibitors of the Proprotein Convertase Furin
2021
Thuy Van Lam van, Miriam Ruth Heindl, Christine Schlutt, Eva Böttcher-Friebertshäuser, Ralf Bartenschlager, Gerhard Klebe, Hans Brandstetter, Sven O Dahms, Torsten Steinmetzer
ACS Medicinal Chemistry Letters
https://doi.org/10.1021/acsmedchemlett.0c00651
https://doi.org/10.1021/acsmedchemlett.0c00651