ID30A-1 / MASSIF-1


A fully automated beamline for the autonomous collection of data from crystals of macromolecules
Status:  open


  • Life Sciences


  • Macromolecular crystallography

Energy range

  • 12.65 - 12.65  keV

Beam size

  • Minimum (H x V) : 10.0 x 10.0  µm²
  • Maximum (H x V) : 100.0 x 100.0  µm²



Technical details

MASSIF1 is a unique facility for the high throughput, fully automatic characterisation and data collection of crystals of macromolecules. The new service is not designed to replace user visits to the synchrotron but rather to do the hard work of screening crystals or collecting data sets through the night, freeing researchers to spend time on more challenging data collection problems and study the underlying biology.

Beam time is booked flexibly and samples then enter a queuing system, users interact with the beamline by describing experimental requirements, that are used by the beamline software to set data collection parameters, in a database, ISPyB, where results are viewed and downloaded as well. The service is made possible by RoboDiff – a new ESRF-developed sample changer that also acts as a goniometer –, a highly intense X-ray beam (5 x 1012 ph/sec in a flexible spot between 100  and 10 µm diameter) and complex workflows that fully evaluate samples, centre the best volumes and collect diffraction data sets optimised for maximum resolution with minimised radiation damage.

  • Svensson, O., Monaco, S., Popov, A. N., Nurizzo, D. & Bowler, M. W. (2015). The fully automatic characterization and data collection from crystals of biological macromolecules, Acta Cryst. D71, 1757-1767
  • Bowler, M.W., Nurizzo, D., et al. (2015). MASSIF-1: A beamline dedicated to the fully automatic characterisation and data collection from crystals of biological macromolecules, J. Synchrotron Rad. 22, 1540-1547
  • Svensson, O., Gilski, M., Nurizzo, D. & Bowler, M. W. (2018) Multi-position data collection and dynamic beam sizing: recent improvements to the automatic data-collection algorithms on MASSIF-1, Acta Cryst. D74, 433-440
  • Bowler, M.W., Svensson, O. & Nurizzo, D. (2016): Fully automatic macromolecular crystallography: the impact of MASSIF-1 on the optimum acquisition and quality of data, Cryst. Rev. 22, 233-249
  • Nurizzo, D., Bowler M.W., et al. (2016) RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments, Acta Cryst D72, 966-975
  • Svensson, O., Gilski, M., Nurizzo, D. & Bowler, M. W. (2019) A comparative anatomy of protein crystals: lessons from the automatic processing of 56,000 samples IUCrJ  6, 822-831

Latest publications

View all publications
Achieving in vivo target depletion through the discovery and optimization of benzimidazolone BCL6 degraders

Bellenie B.R., Cheung K.M.J., Varela A., Pierrat O.A., Collie G.W., Box G.M., Bright M.D., Gowan S., Hayes A., Rodrigues M.J., Shetty K.N., Carter M., Davis O.A., Henley A.T., Innocenti P., Johnson L.D., Liu M., de Klerk S., Le Bihan Y.V., Lloyd M.G., McAndrew P.C., Shehu E., Talbot R., Woodward H.L., Burke R., Kirkin V., van Montfort R.L.M., Raynaud F.I., Rossanese O.W., Hoelder S.,
Journal of Medicinal Chemistry 63, 4047-4068 (2020)