TY - JOUR
T1 - Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV
AU - Gonzalez, Ana
AU - Krojer, Tobias
AU - Nan, Jie
AU - Bjelčić, Monika
AU - Aggarwal, Swati
AU - Gorgisyan, Ishkan
AU - Milas, Mirko
AU - Eguiraun, Mikel
AU - Casadei, Cecilia
AU - Chenchiliyan, Manoop
AU - Jurgilaitis, Andrius
AU - Kroon, David
AU - Ahn, Byungnam
AU - Ekström, John Carl
AU - Aurelius, Oskar
AU - Lang, Dean
AU - Ursby, Thomas
AU - Thunnissen, Marjolein M.G.M.
PY - 2025/5
Y1 - 2025/5
N2 - 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.
AB - 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.
KW - beamlines
KW - BioMAX
KW - drug discovery
KW - FemtoMAX
KW - FragMAX
KW - MicroMAX
KW - protein crystallography
KW - synchrotrons
KW - time-resolved crystallography
UR - https://www.scopus.com/pages/publications/105004939115
U2 - 10.1107/S1600577525002255
DO - 10.1107/S1600577525002255
M3 - Article
C2 - 40184323
AN - SCOPUS:105004939115
SN - 0909-0495
VL - 32
SP - 779
EP - 791
JO - Journal of Synchrotron Radiation
JF - Journal of Synchrotron Radiation
IS - Pt 3
ER -