ID22 - the high-resolution powder-diffraction beamline at ESRF.

Following Phase 2 of the upgrade of the ESRF in which the storage ring was replaced by a new low-emittance ring along with many other facility upgrades, the status of ID22, the high-resolution powder-diffraction beamline, is described. The beamline has an in-vacuum undulator as source providing X-rays in the range 6-75 keV. ID22's principle characteristics include very high angular resolution as a result of the highly collimated and monochromatic beam, coupled with a 13-channel Si 111 multi-analyser stage between the sample and a Dectris Eiger2 X 2M-W CdTe pixel detector.

ID30A-3 (MASSIF-3) - a beamline for macromolecular crystallography at the ESRF with a small intense beam.

ID30A-3 (or MASSIF-3) is a mini-focus (beam size 18 µm × 14 µm) highly intense (2.0 × 10 photons s), fixed-energy (12.81 keV) beamline for macromolecular crystallography (MX) experiments at the European Synchrotron Radiation Facility (ESRF).

ID15A at the ESRF - a beamline for high speed operando X-ray diffraction, diffraction tomography and total scattering.

ID15A is a newly refurbished beamline at the ESRF devoted to operando and time-resolved diffraction and imaging, total scattering and diffraction computed tomography. The beamline is optimized for rapid alternation between the different techniques during a single operando experiment in order to collect complementary data on working systems. The high available energy (up to 120 keV) means that even bulky and highly absorbing systems may be studied.

ID29: a high-intensity highly automated ESRF beamline for macromolecular crystallography experiments exploiting anomalous scattering.

ID29 is an ESRF undulator beamline with a routinely accessible energy range of between 20.0 keV and 6.0 keV (λ = 0.

Diffraction cartography: applying microbeams to macromolecular crystallography sample evaluation and data collection.

Crystals of biological macromolecules often exhibit considerable inter-crystal and intra-crystal variation in diffraction quality. This requires the evaluation of many samples prior to data collection, a practice that is already widespread in macromolecular crystallography. As structural biologists move towards tackling ever more ambitious projects, new automated methods of sample evaluation will become crucial to the success of many projects, as will the availability of synchrotron-based facilities optimized for high-throughput evaluation of the diffraction characteristics of samples.

Protein crystallography with a micrometre-sized synchrotron-radiation beam.

For the first time, protein microcrystallography has been performed with a focused synchrotron-radiation beam of 1 microm using a goniometer with a sub-micrometre sphere of confusion. The crystal structure of xylanase II has been determined with a flux density of about 3 x 10(10) photons s(-1) microm(-2) at the sample. Two sets of diffraction images collected from different sized crystals were shown to comprise data of good quality, which allowed a 1.