Historical background

Abstract

X-ray crystallography was initiated in 1912 by Max von Laue and Peter Ewald. The molecular size and complexity of structures solved by X-ray crystallography gradually increased to include penicillin (Crowfoot, 1948) and vitamin B₁₂ (Hodgkin, 1957). Myoglobin and haemoglobin were the first protein structures to be determined in 1957 and 1959 by Kendrew and Perutz, respectively, using the isomorphous replacement method. The 2 Å resolution structure of myoglobin (Kendrew, 1959) confirmed the right-handed α-helix predicted by Pauling. Subsequently other techniques were added for the structure determination of proteins, including the use of molecular replacement and anomalous dispersion. The increasing power of computers, computer graphics for automation of the `Richards Box' model building system and X-ray production machines have transformed protein crystallography into a vital area of science and a powerful tool for the pharmaceutical industry. This chapter is also available as HTML from the International Tables Online site hosted by the IUCr.