Feature article

More Proteomics...omics...omics...omics...omics

In one of the first examples of the role of crystallography in the new age of proteomics, Sung-Hou Kim and company, [Nature Structural Biology 6, 691-696 (1999)], determined the three dimensional structure of the protein of unknown function from a gene in the sequence of the genome for Methanococcus jannaschii. Half of the predicted gene products of M. jannaschii are unknown. Kim’s determination of the structure has a new fold, part of which is homologous to a nuclear binding protein. The structure suggested biochemical analysis that indicated Mj0226 is a novel nucleotide triphosphatase that hydrolyzes non-standard nucleotides but not standard nucleotides in the presence of Mg2+ or Mn2+ ions. The gene products have sequence homology with predicted gene products in six other species including man, fungus, bacteria and worms. (Welcome to the brave new world. - ed.)

Genome Scoreboard. Genomes OnLine Database tracks the status of over 250 genomes - from Salmonella bacteria to the just-completed human chromosome 21. The links-packed site, which also includes viruses, phages, and organelles, recently found a new home with a company, but will remain free. (igweb.integratedgenomics.com/GOLD) Science, Vol. 288, June 9, 2000

Proteins: Structure, Function and Genetics has inaugurated a new short format of Structure Notes designed to provide brief accounts of X-ray crystal structures that contain 'too little new information to be worthy of publication as a full-length article'. (What do you expect from robots? ed.)

Show Me the Money. Structural GenomiX, a San Diego company that specializes in high throughput x-ray crystallography, completed a second round venture financing that netted $32 million. The company will use the money to continue building a database for analyzing protein structures in drug and compound discovery. The 3-D protein structures the company generates are useful in target validation, rational drug design, pesticide discovery, and industrial catalysis. Drug Design and Development, May 2000

So Simple, A Child Can Do It! 'The crystallography laboratory that you collaborate with produced crystals of your protein weeks ago. They collected X-ray diffraction data and plugged it into their workstation-based molecular-modeling system, coming up with a three-dimensional structure of your protein showing where the component amino acids were located and how they associated with a metallic cofactor at the proteins center.' Holly Ahern, The Scientist Newspaper (Batteries not included, ed.)

Reality Check? In an article entitled 'Protein Crystallography Pinpoints Drug Candidates' (Drug Discovery and Development, April 2000, p26, www.dddmag.com) it's encouraging to read that 'there is nothing simple or straightforward about macromolecular crystallography'. J. Becker, of Merck, and a member of the Industrial Macromolecular Crystallography Assn Collaborative Access Team (twelve pharmaceutical and chemical companies) claims that diffraction analysis lets you see how drugs actually interact with targets. The article summarizes the various steps in macromolecular crystallography and is illustrated with pictures of instruments, molecules and Andy Howard (wearing a smile that could sell used cars).