UNESCO  proclaimed 2014 the International Year of Crystallography. Why? 100 years ago Max von Laue was awarded the Nobel Prize in physics "for his discovery of the diffraction of X-rays by crystals". A year later the father and son Sir William Henry Bragg and William Lawrence Bragg received the Physics prize "for their services in the analysis of crystal structure by means of X-rays”. The International Union of Crystallography has recently counted an astounding 28 Nobel Prizes awarded for research in one way or another related to X-ray crystallography.
It would not be an exaggeration to claim that we are indebted to X-ray crystallography for most of our knowledge on the atomic structure of matter. This of course includes both inorganic and living matter. The contribution of X-ray crystallography to biology probably started with Rosalind Franklin’s and Maurice Wilkins’ experiments, which brought Francis Crick and James Watson to their first insights into the detailed atomic structure of a central player in the cycle of life, DNA. For this they were awarded the Nobel Prize in Physiology or Medicine in 1962. The same year Max Perutz and John Kendrew received the Chemistry prize for the determination of the first protein structure and two years later Dorothy Hodgkin was honored with the Chemistry prize "for her determinations by X-ray techniques of the structures of important biochemical substances”, that is penicillin, Vitamin B12, and insulin.
As we all know, the spectacular achievements in structural biology based on X-ray crystallography have included many highlights, the most recent of which are the Nobel Prize of 2009 to Yonath, Ramakrishnan & Steitz for the structure of the ribosome and the 2012 Prize to Robert J. Lefkowitz and Brian K. Kobilka for the study of the structure and function of GPCRs.
Below are some unique and never published photos, showing some of the pioneers of protein crystallography and Nobel Prize winners with colleagues, both recently and many years before the prizes were awarded!

William Lawrence Bragg during his visit to Uppsala in 1965. Photo provided by Anders Liljas (in the middle on the left).

Dorothy Hodgkin at the International Union for Crystallography (IUCR) meeting in Bordeaux, France, 1990. Photo by S Al-Karadaghi.

Michael Rossmann, one of the pioneers of structural biology, in his famous basement office at Purdue University. Around 1971. Photo by Anders Liljas.

Marin van Heel (on the left, Imperial College, London) and Ada Yonath (Weizmann Institute of Science, Israel), at the Structural Aspects of Protein Synthesis meeting in Tällberg, Sweden, September 1997. Photo by S Al-Karadaghi.

Ada Yonath with colleagues, 9th of December 2009, at the reception at the Royal Swedish Academy of Sciences on the eve prior to the Nobel Prize ceremony. Photo by S Al-Karadaghi.

Peter Moore (Yale University) & Venki Ramakrishnan (MRC Laboratory of Molecular Biology, Cambridge, UK) at the meeting Frontiers in Translation, May 1995, Victoria, Canada. Photo by S Al-Karadaghi.

Brian Kobilka (second left) together with his wife Tong Sun (first on the left) and staff members from the Department of Biochemistry and Structural Biology in Lund, December 2012 (from left: Cecilia Hägerhäll, Per Kjellbom and Ingemar Andre). The Kobilka couple visited Lund during the traditional Chemistry Nobel Prize winners’ trip around Sweden. Photo by S Al-Karadaghi.

The technique of macromolecular X-ray crystallography has of course been evolving throughout the years. Probably the first big change was triggered by the use of synchrotron radiation at the end of the 1980s-beginning of the 1990s. This was followed by the structural genomics initiatives, which brought us new technologies and thousands of new structures. But it did not stop there. Last September I had the privilege to attend two meetings with a focus on current developments in structural biology. The first one was Synchrotron Radiation in Biology, in Hamburg, and the second was the MAX IV Laboratory users meeting in Lund. The MAX-lab meeting included two workshops, one dedicated to the future free electron laser project in Lund while the second to the future MicroMax beamline. MicroMax is going to be the second protein crystallography beamline at the new MAX IV synchrotron in Lund. If I would summarize my general impression from these two meetings in few words, those would be "the new revolution in structural biology". Just a few years ago nobody was talking about “serial crystallography”, and definitely not about collecting a whole data set within a few seconds! Micro-crystallography has made all this possible by targeting crystals with a size of just a few microns and it is essentially driving a fundamental change in the way protein crystallography experiments are run. New technologies in sample handling, data collection and data processing are emerging. This includes, for example, the ability to collect diffraction data directly from crystals in their growth environment, i.e. the crystallization drop. Developments in scanning techniques also allow a quick identification of a single-crystal region in a multi-crystal sample or a well-diffracting region in an imperfect crystal. All this opens up new possibilities for projects where only extremely small crystals can be obtained. The success of the GPCR project, which was awarded the 2012 Nobel Prize, was only possible thanks to the developments in micro-crystallography.
We are entering an exciting new era in structural biology. To this we could of course add the expectations we have in Lund - in two years time we will essentially be walking with our samples to the most advanced synchrotron in the world, MAX IV!

The image below shows the state of the building in December 2013.