Polar bears gave me the idea of how to crystalize ribosomes and consequently to reveal their structure and function. At the beginning, most scientists working on ribosomes concluded that ribosomes cannot be crystallized. I was recovering from an accident and came across an article by a delegation who investigated the metabolism of the winter-sleeping polar bears. As a side finding, they discovered that bear’s ribosomes are periodically packed on the inner side of their cell membranes. This led me to conclude that stress may induce periodic packing, aimed at maintaining the integrity of ribosomes during the winter sleep . Hence I look for ribosomes of bacteria who live under extreme conditions, like in the Dead Sea. This source was indeed suitable for crystallization, but this was not the end of the story, since owing to the extreme sensitivity of the ribosomal crystals to irradiation, we introduced a novel methodology, called cryo bio crystallography, which revolutionized structural biology worldwide. The rest is history. Ultimately, my research was curiosity driven, which kept me active even in low periods. Curiosity, together with passion and love to my family allowed me to progress with a career in science. I feel privileged by my career and consider science a luxury, probably because my family was very poor and I did not expect being paid for working on what I considered my hobby. Having access to the ESRF has been of utmost importance in my research, since we could obtain the data required for determining the ribosome structure. In fact, many of our publications are based on data collected at the ESRF. Obviously, I am extremely happy to see that the ESRF is maintaining itself as a state-of-the-art facility, like the recent installation of a cryo-electron microscope, a tool that currently revolutionises structural biology.