Structural biology

Protein crystallography has become a major technique for understanding cell ular processes. This has come about through great advances in the technolog y of data collection and interpretation, particularly the use of synchrotro n radiation. The ability to express eukaryotic genes in Escherichia coli is also important. Analysis of known structures shows that all proteins are b uilt from about 1000 primeval folds. The collection of all primeval folds p rovides a basis for predicting structure from sequence. At present about 45 0 are known. Of the presently sequenced genomes only a fraction can be rela ted to known proteins on the basis of sequence alone. Attempts are being ma de to determine all (or as many as possible) of the structures from some ba cterial genomes in the expectation that structure will point to function mo re reliably than does sequence. Membrane proteins present a special problem . The next 20 years may see the experimental determination of another 40000 protein structures. This will make considerable demands on synchrotron sou rces and will require many more biochemists than are currently available. T he availability of massive structure databases will alter the way biochemis try is done.