[1][2][3] A new replacement building constructed close by to the original site on the Cambridge Biomedical Campus was opened by Queen Elizabeth II in May 2013.

[4] The road outside the new building is named Francis Crick Avenue after the 1962 joint Nobel Prize winner and LMB alumnus, who co-discovered the helical structure of DNA in 1953.

[5] Max Perutz, following undergraduate training in organic chemistry, left Austria in 1936 and came to the University of Cambridge to study for a PhD, joining the X-ray crystallographic group led by J.D.

The death of Lord Rutherford led to his successor, Lawrence Bragg, a pioneer in X-ray crystallography, becoming the new Cavendish professor of physics in 1938.

After World War II, many scientists from the physical side of science turned to biology, bringing with them a new way of thinking and expertise.

Perutz discovered that the detailed three-dimensional structures of proteins, such as myoglobin and hemoglobin could, in principle, be solved by X-ray analysis using a heavy metal atom labeling technique.

Also that year, Vernon Ingram discovered that the disease sickle cell anaemia is caused by a single amino acid change in the hemoglobin molecule and Sydney Brenner joined the Unit.

In 1961 Brenner helped discover messenger RNA and, in the same year, he and Crick established that the genetic code was read in triplets.

Additionally, Fred Sanger's Unit which had been housed in the university's Biochemistry department joined them, as did Aaron Klug from London.

[7] The new LMB had Perutz as its chairman and contained 3 divisions: Structural Studies, headed by Kendrew; Molecular Genetics (Crick); Protein Chemistry (Sanger).

The atomic structure of the first tRNA molecule was solved and zinc fingers discovered by Klug (who received the Nobel Prize for Chemistry in 1982).

Sulston determined the cell lineage of this small worm and John Graham White the entire wiring diagram of its nervous system.

Peter Lawrence came to study pattern formation, helping discover how compartments in Drosophila determine the fly's body plan.

This fundamental discovery is the keystone to understanding the molecular mechanism by which organisms can produce a diverse repertoire of antibodies to recognise new pathogens.

Finally, the molecular mechanisms elucidated by Neuberger may be of great importance in understanding the mutational pattern of kataegis in breast cancer.

Richard Henderson and Nigel Unwin developed electron crystallography to determine the structure of two-dimensional arrays, applying this to the bacterial purple protein, bacteriorhodopsin.

Some major examples include nucleic acid sequencing, protein and antibody engineering, construction of new X-ray equipment and the invention of the scanning confocal microscope.

[16] From outside the LMB, the parent MRC ensured that the quinquennial assessment had a light touch: only a brief explanation of past achievements and an indication of where future plans lay were required by the external committee.