MicroMAX will open up new possibilities in the area of structural biology making it possible to study proteins in 3D and to follow them in time. MicroMAX will allow studying the molecules that are most interesting but most difficult to study such as membrane proteins and molecular complexes. This will be achieved by providing a very small but parallel and intense X-ray beam and by making it possible to use new methods of presenting the samples to the X-ray beam. The technique used is called X-ray crystallography: by making a crystal of the protein that we would like to study, illuminating it with an X-ray beam and recording the scattered X-rays it is possible to obtain a 3D-model of the protein.

The science of structural biology studies structures of biological molecules with the goal to understand how biology works on a molecular level. The function of these molecules is determined by their structure, and since most functions in for example our cells is carried out by these molecules it is fundamental to understanding life.

Membrane proteins are embedded in for example the membrane separating the interior of cells from the exterior and therefore crucial for the interaction of cells with other cells and the outside world. Membrane proteins are one of the largest classes of drug targets, i.e. the proteins that medical drugs bind to in order to do their job. It is more difficult to make crystals of membrane proteins and often the result is very small crystals that requires an X-ray beam of around one millionth of a metre in diameter.

The function of proteins is often accomplished by binding to one or many other proteins or nucleic acids (such as DNA that encode our genes). These molecular complexes are often more difficult to study for many reasons. For example, their large size makes the signal from the crystals very weak.

MicroMAX is expected to be in user operation in 2022.

MicroMAX has been funded by the Novo Nordisk Foundation.

Contact Info: Thomas Ursby

Techniques Macromolecular Serial Crystallography with a wide range of sample delivery systems, time-resolved studies
Beam Size Tunable between below 1 μm up to 10 μm (FWHM, horizontal and vertical)
Energy Range 5–30 keV (0.4 –2.5 Å)
Time Scales Down to microseconds
Samples Microcrystals of biological molecules


HALOS – A unique collaboration in Life Science

A new EU project in the program area Öresund-Kattegatt-Skagerak (ÖKS) has been approved. The Hanseatic League of Science (HALOS) will build a unique collaboration between Hamburg and South-West Scandinavia, bring together the four unique research facilities MAX IV, ESS, DESY and European XFEL, and create a centre for integrated, world-leading Life Science innovation and research.