Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV
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 se...
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| Format: | Article |
| Language: | English |
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International Union of Crystallography
2025-05-01
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| Series: | Journal of Synchrotron Radiation |
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| Online Access: | https://journals.iucr.org/paper?S1600577525002255 |
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| author | Ana Gonzalez Tobias Krojer Jie Nan Monika Bjelčić Swati Aggarwal Ishkan Gorgisyan Mirko Milas Mikel Eguiraun Cecilia Casadei Manoop Chenchiliyan Andrius Jurgilaitis David Kroon Byungnam Ahn John Carl Ekström Oskar Aurelius Dean Lang Thomas Ursby Marjolein M. G. M. Thunnissen |
| author_facet | Ana Gonzalez Tobias Krojer Jie Nan Monika Bjelčić Swati Aggarwal Ishkan Gorgisyan Mirko Milas Mikel Eguiraun Cecilia Casadei Manoop Chenchiliyan Andrius Jurgilaitis David Kroon Byungnam Ahn John Carl Ekström Oskar Aurelius Dean Lang Thomas Ursby Marjolein M. G. M. Thunnissen |
| author_sort | Ana Gonzalez |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-7e618bb7542146c6bcfdb8144a9a7865 |
| institution | Kabale University |
| issn | 1600-5775 |
| language | English |
| publishDate | 2025-05-01 |
| publisher | International Union of Crystallography |
| record_format | Article |
| series | Journal of Synchrotron Radiation |
| spelling | doaj-art-7e618bb7542146c6bcfdb8144a9a78652025-08-20T03:52:52ZengInternational Union of CrystallographyJournal of Synchrotron Radiation1600-57752025-05-0132377979110.1107/S1600577525002255sze5001Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IVAna Gonzalez0Tobias Krojer1Jie Nan2Monika Bjelčić3Swati Aggarwal4Ishkan Gorgisyan5Mirko Milas6Mikel Eguiraun7Cecilia Casadei8Manoop Chenchiliyan9Andrius Jurgilaitis10David Kroon11Byungnam Ahn12John Carl Ekström13Oskar Aurelius14Dean Lang15Thomas Ursby16Marjolein M. G. M. Thunnissen17MAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenMAX IV Laboratory, Lund University, Fotongatan 2, Lund 224 84, SwedenThe 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.https://journals.iucr.org/paper?S1600577525002255protein crystallographysynchrotronsbeamlinestime-resolved crystallographydrug discoverybiomaxmicromaxfragmaxfemtomax |
| spellingShingle | Ana Gonzalez Tobias Krojer Jie Nan Monika Bjelčić Swati Aggarwal Ishkan Gorgisyan Mirko Milas Mikel Eguiraun Cecilia Casadei Manoop Chenchiliyan Andrius Jurgilaitis David Kroon Byungnam Ahn John Carl Ekström Oskar Aurelius Dean Lang Thomas Ursby Marjolein M. G. M. Thunnissen Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV Journal of Synchrotron Radiation protein crystallography synchrotrons beamlines time-resolved crystallography drug discovery biomax micromax fragmax femtomax |
| title | Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV |
| title_full | Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV |
| title_fullStr | Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV |
| title_full_unstemmed | Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV |
| title_short | Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV |
| title_sort | status and perspective of protein crystallography at the first multi bend achromat based synchrotron max iv |
| topic | protein crystallography synchrotrons beamlines time-resolved crystallography drug discovery biomax micromax fragmax femtomax |
| url | https://journals.iucr.org/paper?S1600577525002255 |
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