ID30A-3 / MASSIF-3

Synopsis

MASSIF-3 is a minifocus beamline (15 µm diameter), operating at fixed energy (12.81 keV). The beamline is dedicated to protein crystals of small size, inhomogeneous protein crystals, and fast data collection, and is also suitable for SAD measurements (Se, Pt, Au,...). MASSIF-3 is equipped with a MD2 micro-diffractometer and with a FlexHCD sample changer for SPINE pucks and UniPucks. Diffraction data are recorded on an Eiger1 X 4M detector that allows data collection at a very high frame rate (up to 750 Hz). The high resolution limit on the beamline is 1.17 Å.

Status: open

Disciplines

Medicine
Life Sciences
Chemistry
Environmental Sciences

Applications

Macromolecular crystallography
Time resolved serial oscillation crystallography (SOX)

Techniques

MX - Macromolecular Crystallography
XRD - X-ray Diffraction
TR-XRD - Time Resolved X-ray Diffraction
TR-MX - Time-Resolved Macromolecular Crystallography
SMX - Serial Macromolecular Crystallography
SCXRD - Single Crystal X-ray Diffraction, SC-XRD, SCD, SXRD
SAD - Single-wavelength Anomalous Diffraction

Energy range

12.81 keV

Beam size

Minimum (H x V) : 15.0 x 15.0 µm²
Maximum (H x V) : 15.0 x 15.0 µm²

Sample environments

100 K cryostream
automatic sample changer
dehydration device
online microspec

Detectors

Eiger1 X 4M

Technical details

High resolution limit - 1.17Å

References:

ID30A-3 (MASSIF-3) – a beamline for macromolecular crystallography at the ESRF with a small intense beam, D. Von Stetten et al., J. Synchrotron Radiat. (2020) 27: 844–851. doi: 10.1107/S1600577520004002

The Upgrade Programme for the Structural Biology beamlines at the European Synchrotron Radiation Facility – High throughput sample evaluation and automation, P. Theveneau et al. (2013) J. Phys.: Conf. Ser. 425 012001 doi:10.1088/1742-6596/425/1/012001

Latest publications

View all publications

Structural and binding studies of the mycobacterial heat shock protein reveal a silent state and offer insights into dendritic cell activation

Barra G., Sala M., Scala M.C., Campiglia P., Kim H.J., Ruggiero A., Berisio R.,
International Journal of Biological Macromolecules 353, 151218-1-151218-11 (2026)

Computational enzyme design by catalytic motif scaffolding

Braun M., Tripp A., Chakatok M., Kaltenbrunner S., Fischer C., Stoll D., Bijelic A., Elaily W., Totaro M.G., Moser M., Hoch S.Y., Lechner H., Rossi F., Aleotti M., Hall M., Oberdorfer G.,
Nature 649, 237-245 (2026)

Exploring dual inhibitors Carbonic Anhydrases and Phosphodiesterase 5 as potential agents for treatment Alzheimer's disease

Costa A., Provensi G., Titi C., Leri M., Bucciantini M., Ferraroni M., Keeton A.B., Moore A.M., Piazza G.A., Abadi A.H., Angeli A., Supuran C.T.,
European Journal of Medicinal Chemistry 303, 118404-1-118404-18 (2026)

An integrated structural and functional profiling approach uncovers the mechanisms of pregnane X receptor binding and activation by pharmaceutical and environmental compounds

Derosa Q., Carivenc C., Sirounian S., Grimaldi M., Boulahtouf A., Delfosse V., Balaguer P., Bourguet W.,
Molecular Pharmacology 108, 100140-1-100140-11 (2026)

Outer membrane–peptidoglycan anchoring in Pseudomonas aeruginosa

El-Araby A.M., Pérez de José U., Miguel-Ruano V., Lee M., Feltzer R., Avila-Cobian L.F., Hesek D., Fisher J.F., Hermoso J.A., Mobashery S.,
Journal of the American Chemical Society 148, 25740-25756 (2026)

Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1

Favre S., Pillet B., Burchert F., Siva Sankar D., Méndez-Godoy A., Kiontke S., Dengjel J., Bange G., Kressler D.,
Nucleic Acids Research 54, gkag264-1-gkag264-41 (2026)