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X-Ray crystallography is nowadays an accurate and rapid method of determining conformation in the crystal lattice, which conformation usually corresponds to the preferred conformation in solution.

The basic structure of proteins is quite simple: they are formed by hooking together in a chain discrete subunits called amino acids.

Much of my work in biology has been driven by my early training in chemistry. When studying a new chemical compound, the first and most important thing is to determine its detailed molecular structure.

In many biological structures proteins are simply components of larger molecular machines.

This work made me more and more interested in biological matter, and I decided that I really wanted to work on the X-ray analysis of biological molecules.

These studies resulted eventually in a complete sequence analysis of the complex from several species, and in the atomic resolution structure of the F catalytic domain of the enzyme from bovine mitochondria, giving new insights into how ATP is made in the biological world.

The success in the determination of the high-resolution structures of ribosomal subunits and eventually the whole ribosome was the culmination of decades of effort.

Owing to the difficulty of dealing with substances of high molecular weight we are still a long way from having determined the chemical characteristics and the constitution of proteins, which are regarded as the principal con-stituents of living organisms.

During the decade following the discovery of the double-helical structure of DNA, the problem of translation - namely, how genetic information is used to synthesize proteins - was a central topic in molecular biology.

Broadly speaking, the discovery of X-rays has increased the keenness of our vision ten thousand times, and we can now 'see' the individual atoms and molecules.