Crystals on the cover

PO Box 6395, Lawrenceville, NJ 08648-0395, USA, and School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia The cover of this issue of Acta Crystallographica Section F is the third one to display a photomontage of crystal micrographs. Section F has committed its cover illustration for the January issue each year to a highlight of its crystallization content with an artful assembly of the best in crystal photomicrographs submitted by authors of crystallization communications published the year before. As a reminder, authors are asked to nominate published photographs of crystals themselves. If authors would like one of their published photographs considered as part of a future crystals cover, they should alert Technical Editor, Louise Jones ([email protected]) by e-mail. The nomination process must be completed by 1 December in order to assemble the final collage in time for the January issue (December photographs will be eligible for consideration for the cover of the following year). Selection factors include focus, contrast, color and symmetry, but, in the final assembly, the chosen photographs must be complementary to one another. The papers providing micrographs for this year’s cover are all from Acta Cryst. F63 (2007) and details are as follows. Top row: putative zinc transporter CzrB from Thermus thermophilus (Höfer et al., pp. 673–677); the fluoresecent probe tetrasulfocyanine in complex with the Fab antibody fragment MOR03268 (Hillig et al., pp. 217–223); and the homing endonuclease I-Dmo-I in complex with its target DNA (Redondo et al., pp. 1017–1020). Middle row: an Escherichia coli tRNA acceptor-stem microhelix (Förster et al., pp. 46–48); BigR, a transcription repressor from Xylella fastidiosa (Barbosa et al., pp. 596–598); and PH1010 from Pyrococcus horikoshii OT3 (Shirokane et al., pp. 532–534). Bottom row: the N-terminal region of the human formin-homology protein FHOD1 (Schulte et al., pp. 878–881); the archaeal transcription termination factor NusA (Tanaka et al., pp. 69–73); and Escherichia coli WrbA in complex with its cofactor flavin mononucleotide (Wolfová et al., pp. 571–575). Last year, one of us attended the biennial Recent Advances in Macromolecular Crystallization meeting (http://www.hamptonresearch.com/stuff/ RAMC.aspx) in San Diego, California. The strictly small scale, the helpful workshop, the rich program of timely presentations, the inventive tools for encouraging discussion and, above all, the enthusiastic participation of attendees and organizers alike make this a unique and most rewarding experience for everyone who attends. This year, the twelfth in the series of the biennial ICCBM meetings (http://www.iquimica.unam.mx/ICCBM12/) will be held, this one being in Cancun, Mexico. The ICCBM meetings cover the widest range of topics of crystallization import, including, for example, developments in high-throughput methods for structural genomics, and are traditionally preceded by a workshop on basic crystallization methods. These meetings, the RAMC and the ICCBM meetings, are a great service to the crystallization community. The organizers deserve our thanks and support. Anyone with an interest in macromolecular crystallization is encouraged to attend. Acta Crystallographica Section F Structural Biology and Crystallization Communications