Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV
(2025) In Journal of Synchrotron Radiation 32(Pt 3). p.779-791- Abstract
The first multi-bend achromat based synchrotron MAX IV operates two protein crystallography beamlines, BioMAX and MicroMAX. BioMAX is designed as a versatile, stable, high-throughput beamline catering for most protein crystallography experiments. MicroMAX is a more ambitious beamline dedicated to serial crystallography including time-resolved experiments. Both beamlines exploit the special characteristics of fourth-generation beamlines provided by the 3 GeV ring of MAX IV. In addition, the fragment-based drug discovery platform, FragMAX, is hosted and, at the FemtoMAX beamline, protein diffraction experiments exploring ultrafast time resolution can be performed. A technical and operational overview of the different beamlines and the... (More)
The first multi-bend achromat based synchrotron MAX IV operates two protein crystallography beamlines, BioMAX and MicroMAX. BioMAX is designed as a versatile, stable, high-throughput beamline catering for most protein crystallography experiments. MicroMAX is a more ambitious beamline dedicated to serial crystallography including time-resolved experiments. Both beamlines exploit the special characteristics of fourth-generation beamlines provided by the 3 GeV ring of MAX IV. In addition, the fragment-based drug discovery platform, FragMAX, is hosted and, at the FemtoMAX beamline, protein diffraction experiments exploring ultrafast time resolution can be performed. A technical and operational overview of the different beamlines and the platform is given as well as an outlook for protein crystallography embedded in the wider possibilities that MAX IV offers to users in the life sciences.
(Less)
- author
- organization
- publishing date
- 2025-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- beamlines, BioMAX, drug discovery, FemtoMAX, FragMAX, MicroMAX, protein crystallography, synchrotrons, time-resolved crystallography
- in
- Journal of Synchrotron Radiation
- volume
- 32
- issue
- Pt 3
- pages
- 13 pages
- publisher
- International Union of Crystallography
- external identifiers
-
- pmid:40184323
- scopus:105004939115
- ISSN
- 0909-0495
- DOI
- 10.1107/S1600577525002255
- language
- English
- LU publication?
- yes
- id
- 499e1ea4-9812-41fb-b24f-bd5c3103c636
- date added to LUP
- 2025-08-04 12:59:28
- date last changed
- 2025-08-04 13:00:13
@article{499e1ea4-9812-41fb-b24f-bd5c3103c636, abstract = {{<p>The first multi-bend achromat based synchrotron MAX IV operates two protein crystallography beamlines, BioMAX and MicroMAX. BioMAX is designed as a versatile, stable, high-throughput beamline catering for most protein crystallography experiments. MicroMAX is a more ambitious beamline dedicated to serial crystallography including time-resolved experiments. Both beamlines exploit the special characteristics of fourth-generation beamlines provided by the 3 GeV ring of MAX IV. In addition, the fragment-based drug discovery platform, FragMAX, is hosted and, at the FemtoMAX beamline, protein diffraction experiments exploring ultrafast time resolution can be performed. A technical and operational overview of the different beamlines and the platform is given as well as an outlook for protein crystallography embedded in the wider possibilities that MAX IV offers to users in the life sciences.</p>}}, author = {{Gonzalez, Ana and Krojer, Tobias and Nan, Jie and Bjelčić, Monika and Aggarwal, Swati and Gorgisyan, Ishkan and Milas, Mirko and Eguiraun, Mikel and Casadei, Cecilia and Chenchiliyan, Manoop and Jurgilaitis, Andrius and Kroon, David and Ahn, Byungnam and Ekström, John Carl and Aurelius, Oskar and Lang, Dean and Ursby, Thomas and Thunnissen, Marjolein M.G.M.}}, issn = {{0909-0495}}, keywords = {{beamlines; BioMAX; drug discovery; FemtoMAX; FragMAX; MicroMAX; protein crystallography; synchrotrons; time-resolved crystallography}}, language = {{eng}}, number = {{Pt 3}}, pages = {{779--791}}, publisher = {{International Union of Crystallography}}, series = {{Journal of Synchrotron Radiation}}, title = {{Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV}}, url = {{http://dx.doi.org/10.1107/S1600577525002255}}, doi = {{10.1107/S1600577525002255}}, volume = {{32}}, year = {{2025}}, }