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Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV

Gonzalez, Ana LU ; Krojer, Tobias LU orcid ; Nan, Jie LU orcid ; Bjelčić, Monika LU ; Aggarwal, Swati LU ; Gorgisyan, Ishkan LU ; Milas, Mirko LU ; Eguiraun, Mikel LU ; Casadei, Cecilia LU and Chenchiliyan, Manoop LU , et al. (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.

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organization
publishing date
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
  • scopus:105004939115
  • pmid:40184323
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
2025-08-18 14:09:44
@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}},
}