Significant improvements to the sample-location, characterization and data-collection algorithms on the autonomous ESRF beamline MASSIF-1 are described. The workflows now include dynamic beam-diameter adjustment and multi-position and multi-crystal data collections.

A fully automatic system has been developed that performs X-ray centring and characterization of, and data collection from, large numbers of cryocooled crystals without human intervention.

MASSIF-1 (ID30A-1) is a new beamline dedicated to the completely automatic characterization and data collection from crystals of biological macromolecules.

An industrial six-axis robot has been combined with a high-accuracy air-bearing rotation axis to create a single device with the capabilities of both transferring cryocooled protein crystals from a sample-containing dewar and collecting complete X-ray diffraction data sets.

The intrinsic variability between and within macromolecular crystals has a large effect on screening and data-collection strategies. Measures of this variability and their implications for data collection are presented.

New tools for the evaluation of the diffraction characteristics of crystals of macromolecules are presented in the context of the ESRF Upgrade MASSIF beamlines.

A powerful and easy-to-use workflow environment has been developed at the ESRF for combining experiment control with online data analysis on synchrotron beamlines. This tool provides the possibility of automating complex experiments without the need for expertise in instrumentation control and programming, but rather by accessing defined beamline services.

A system for the automatic reduction of single- and multi-position macromolecular crystallography data is presented.