Notable

K. Rein et al., "The Drosophila standard brain," Current Biology, 12[3]:227-31, Feb. 5, 2002. "The authors present an approach to create a 3D image of the fly brain. This is a very useful resource tool that will make it possible to create an atlas of gene expression patterns and will be very useful for analyzing brain structure in mutant backgrounds." —Oliver Hobert, Columbia University College of Physicians and Surgeons, US X-Ray Crystallography F.J. Lopez-Jaramillo et al., "Crystallization and cryocrystallography inside X-ray capillaries," Journal of Applied Crystallography, 34:365-370, 2001. "Isolated crystals are grown in a gelled agarose-protein solution inside X-ray capillaries, cryoprotected with glycerol inside the same capillary, and X-rayed inside the same capillary. Performing all of the growing and imaging functions inside the same reactor minimizes crystal handling and permits analysis at different temperatures or other conditions. The authors present a laser pointer system to illuminate the crystal to be flash-cooled to minimize icing and misalignment of the crystal." —Deirdre Meldrum, University of Washington, US S. Faham, J.U. Bowie, "Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure,"Journal of Molecular Biology, 316[1]:1-6, Feb. 8, 2002. "Integral membrane proteins are generally crystallized using either detergents or lipids, but this paper describes a new approach which uses a mixture of both. Bicelles, or bilayer micelles, formed from mixtures of lipid and detergent, have been used to orient soluble protein samples for NMR [nuclear magnetic resonance] experiments. In this paper, the method is applied to crystallizing bacteriorhodpsin. The lipid/detergent mixtures are generally fluid at low temperatures, but develop a gel-like consistency at higher temperatures. Because gelling occurs at 37o Celsius, this method will not be appropriate for all membrane proteins, but the method is a simple and novel approach to be added to the other crystallization techniques currently in use." —Susan Buchanan, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US DNA Methylation F. Santos et al., "Dynamic reprogramming of DNA methylation in the early mouse embryo," Developmental Biology, 241[1]:172-82, Jan. 1, 2002. "This paper provides many valuable observations of the dynamics of methylation and chromatin structure/remodeling in the early post-fertilization mammalian embryo. This analysis of male pronuclear demethylation, protamine-histone exchange and de novo methylation during early development will aid in a more complete understanding of nuclear remodeling and transcriptional dynamics." —Mark Westhusin, Texas A+M University, US SNP Genotyping S. Sauer et al., "Facile method for automated genotyping of single nucleotide polymorphisms by mass spectrometry," Nucleic Acids Research, 30[5]:22, March 1, 2002. "The development of automated, accurate and cheap methods for typing single nucleotide polymorphisms (SNPs) is a critical component of progress in the identification of susceptibility genes for complex disorders. This [study] describes important improvements to the "GOOD" assay for SNP typing by mass spectrometry, which has now been simplified to a single-tube, three-step method which does not require purification of reaction products. A key advance is the use of a novel DNA polymerase, Tma 31 FS, which preferentially incorporates ddNTPs over dNTPs in the primer extension reaction." —Christopher Mathew, Guy's, King's & St. Thomas' School of Medicine, UK E. Genin, "Selection of single nucleotide polymorphisms for association studies in candidate genes," Genetic Epidemiology, 21 Suppl. 1:S614-9, 2001. "For case-control disease association studies, the author proposes a mathematical method to select a subset of all single nucleotide polymorphisms (SNPs) in a gene. To keep costs of genotyping at reasonable levels, selecting a subset of markers for analysis is an important consideration in the planning of an association study. Interestingly, power of analysis can be higher when only a subset of markers as opposed to all markers are used." —Jurg Ott, The Rockefeller University, US "RNomics" T.H. Tang et al., "RNomics in Archaea reveals a further link between splicing of archaeal introns and rRNA processing," Nucleic Acids Research, 30[4]:921-30, Feb. 15, 2002. "RNomics attempts to identify all small non-mRNA species and their genes in various organisms. [The authors' research] reveals surprising links between the endonucleolytic splicing of introns in tRNAs and ribosomal rRNA processing in two representatives of major archaeal kingdoms, the Euryarchaeota and the Crenarchaeota. The archaeal splicing endonuclease possesses a characteristic recognition motif which exists both at the exon/intron junctions in tRNAs and in the archaeal primary rRNA transcripts. In this paper, it is shown that the processes occurring during rRNA maturation are the same as those occurring in intron splicing of tRNAs with re-ligation and formation of circular products. Interestingly, a spliced product contains a box C/D motif, hallmark of C/D box snoRNAs directing 2'-O-methylation of specific riboses in rRNAs, which is shown to bind the L7Ae protein, a core component of archaeal C/D box snoRNPs also present in the 50S ribosomal subunit of H. marismortui. The following paper [in the journal] (J.F. Kuhn et al., "Archaeal ribosomal protein L7 is a functional homolog of the eukaryotic 15.5kD/Snu13p snoRNP core protein," Nucleic Acids Research, 30, 931, 2002) demonstrates independently and elegantly that L7Ae is the functional homolog of the eukaryotic 15.5 kD C/D snoRNP protein." —Eric Westhof, Institut de Biologie Moleculaire et Cellulaire du CNRS, France

Notable

X-Ray Crystallography

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