FemtoMAX – an X-ray beamline for structural dynamics at the short-pulse facility of MAX IV

Enquist, Henrik; Jurgilaitis, A.; Jarnac, Amélie; Bengtsson, Anders; Burza, Matthias; Curbis, Francesca; Disch, C.; Ekström, Johanna; Harb, Maher; Isaksson, L.; Kotur, Marija; Kroon, David; Lindau, Filip; Mansten, Erik; Nygaard, Jesper; Persson, Ann; Pham, Van Tuong; Rissi, M.; Thorin, Sara; Tu, Chien Ming; Wallén, Erik; Wang, Xiaocui; Werin, Sverker; Larsson, Jörgen

doi:10.1107/s1600577517017660

Cited by 18 publications

(20 citation statements)

References 31 publications

(24 reference statements)

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“…The facility has, presently, 16 funded beamlines of which ten are situated at the 3 GeV ring. The first beamlines to run commissioning experiments were BioMAX, the nano-science beamline NanoMAX (Johansson et al, 2018) and the structural dynamics beamline FemtoMAX (Enquist et al, 2018) at the short pulse facility.…”

Section: Introductionmentioning

confidence: 99%

BioMAX – the first macromolecular crystallography beamline at MAX IV Laboratory

Ursby

Åhnberg

Appio

et al. 2020

J Synchrotron Radiat

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BioMAX is the first macromolecular crystallography beamline at the MAX IV Laboratory 3 GeV storage ring, which is the first operational multi-bend achromat storage ring. Due to the low-emittance storage ring, BioMAX has a parallel, high-intensity X-ray beam, even when focused down to 20 µm × 5 µm using the bendable focusing mirrors. The beam is tunable in the energy range 5–25 keV using the in-vacuum undulator and the horizontally deflecting double-crystal monochromator. BioMAX is equipped with an MD3 diffractometer, an ISARA high-capacity sample changer and an EIGER 16M hybrid pixel detector. Data collection at BioMAX is controlled using the newly developed MXCuBE3 graphical user interface, and sample tracking is handled by ISPyB. The computing infrastructure includes data storage and processing both at MAX IV and the Lund University supercomputing center LUNARC. With state-of-the-art instrumentation, a high degree of automation, a user-friendly control system interface and remote operation, BioMAX provides an excellent facility for most macromolecular crystallography experiments. Serial crystallography using either a high-viscosity extruder injector or the MD3 as a fixed-target scanner is already implemented. The serial crystallography activities at MAX IV Laboratory will be further developed at the microfocus beamline MicroMAX, when it comes into operation in 2022. MicroMAX will have a 1 µm × 1 µm beam focus and a flux up to 1015 photons s−1 with main applications in serial crystallography, room-temperature structure determinations and time-resolved experiments.

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Section: Introductionmentioning

confidence: 99%

BioMAX – the first macromolecular crystallography beamline at MAX IV Laboratory

Ursby

Åhnberg

Appio

et al. 2020

J Synchrotron Radiat

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“…We irradiate the crystal with X-rays produced by a multilayer monochromator and treat the resulting streaky diffraction patterns with a software originally designed for monochromatic diffraction and oscillation data collection (XDS) (Kabsch, 2010). An untested aspect of this work is the use of time-over-threshold (ToT) detector mode of the pixel array detector, for recording diffraction intensities from protein crystals (Enquist et al, 2018). We show that it is possible to model individual isotropic B-factors of atoms based on the protein diffraction data obtained at the FemtoMAX beamline.…”

Section: Introductionmentioning

confidence: 99%

High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection

Jensen

Gagnér

Sanchez

et al. 2021

J Synchrotron Radiat

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Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative intensity distribution compared with theoretical distribution, I/σ, R merge/R meas and CC1/2 statistics versus resolution. The FemtoMAX beamline provides an interesting alternative to X-ray free-electron lasers when studying reversible processes in protein crystals.

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“…While alternative sources such as free-electron lasers (McNeil & Thompson, 2010;Helml et al, 2014) or laboratory setups (Weisshaupt et al, 2014;Bargheer et al, 2004) of picosecond (or shorter) X-ray pulses are generally available, they are either difficult to access or provide only low flux compared with synchrotron radiation. Consequently, an increasing number of medium/hard X-ray scattering beamlines around the world have expanded their portfolio towards laserpumped experiments, addressing new scientific questions (March et al, 2011;Wang et al, 2017;Navirian et al, 2012;Enquist et al, 2018;Wulff et al, 2003;Sun et al, 2016).…”

Section: Introductionmentioning

confidence: 99%