FEBS Journal

© Federation of European Biochemical Societies

Cover image for Vol. 279 Issue 4

Edited By: Richard Perham

Impact Factor: 3.129

ISI Journal Citation Reports © Ranking: 2010: 124/286 (Biochemistry & Molecular Biology)

Online ISSN: 1742-4658

Virtual Issue Structural Biology


May 2009 Virtual Issue Structural Biology

Papers Selected by Alex Wlodawer

Front cover: Fig 2a from G. Meriläinen, FEBS J 275 pp 6136-6148

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Introduction

We are in the midst of celebrating 50 years of protein crystallography, counted from publication of the preliminary and complete structures of myoglobin [1,2]. During the first few years of the application of this technique the appearance of each new structure was a major event and was usually published in journals that are now considered to be in the “high impact” category. Much has changed since then as the number of macromolecular structures deposited in the Protein Data Bank (PDB) now exceeds 50,000. Although some of them were solved using NMR or even electron microscopy, a vast majority still resulted from crystallographic investigations. A new (and rather disturbing) development is that many novel structures, solved in various centers for structural genomics, are only available as PDB entries, since they are not being published in peer-reviewed literature at all. Under these circumstances, one could ask about the role of a general-interest biochemistry journal, such as this one, in publishing the results of investigations that utilize protein crystallography as their major experimental technique. Also, how is it that, according to a recent analysis [3], the technical quality of the structures published in the FEBS Journal appears to be among the highest among all journals? An answer can be found in the papers selected for this Virtual Issue, which give a cross-section of articles that featured crystallographic investigations and were published in 2008 and 2009. Several of these papers are reviews aimed at providing the readers with either the ways of critically interpreting crystal structures, or with detailed comparative analyses of particular families of proteins, based on multiple crystal structures of their members. A vast majority of the structures presented in original articles were solved using molecular replacement with models based on related proteins. Although these structures may not be truly novel, they are often very important, since they can elucidate enzymatic properties through analysis of inhibitor binding, compare related proteins from several species with the aim of creating selective inhibitors, or explain the biophysical properties such as thermostability or cold adaptation. Such results are crucial in both enhancing our understanding of the ways protein fold and work, as well as in practical applications such as drug design. Some structures published here are still solved from scratch through the application of methods such as isomorphous replacement or anomalous scattering, and they represent proteins with less well studied folds. What is not shown in this Virtual Issue are many papers (actually, a fairly large fraction of all papers published in this journal) that contain figures showing protein structures that are used to interpret a variety of biological, biochemical, or biophysical data, although these papers do not report crystallographic studies at all. The fact that the availability of crystal structures is now taken completely for granted and that such structures are routinely used for interpretation of a wide range of phenomena testifies to the success of the last 50 years of macromolecular crystallography.

References

  1. Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, & Phillips DC (1958) A three-dimensional model of the myoglobin molecule obtained by x-ray analysis. Nature 181, 662-666.

  2. Kendrew JC, Dickerson RE, Strandberg BE, Hart RG, Davies DR, Phillips DC, & Shore VC (1960) Structure of myoglobin. A three-dimensional fourier synthesis at 2 Å resolution. Nature 185, 422-427.

  3. Brown EN & Ramaswamy S (2007) Quality of protein crystal structures. Acta Crystallogr D63, 941-950.


Review Articles

Original Articles


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