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Newsletter 141 February 12, 2007 |
The
NIH X-Ray Diffraction
Interest Group
Newsletter
web site: http://mcl1.ncifcrf.gov/nihxray
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Happy Birthday, Dr. Davies Alexander Wlodawer (NCI): It may be hard to believe, but David Davies will be celebrating his 80th
birthday on Feb. 22nd, 2007. There is no need to tell this audience who David is
and what he has accomplished - those that do not know must have been asleep for
a very long time. Ten years ago, NIH honored his previous round birthday with a
one-day symposium. Such symposia, however, might be taken like
an invitation to retire, and David did not express any desire for such a step,
either then or now. Thus, there is no symposium this time, to make sure that
David will not decide to abandon his work any time soon. David, we appreciate
the example that you gave us, the superb science that you produced, and your
leadership role in the NIH community, as well as in the larger community of
structural biologists in the US and abroad. We would like to wish you many more
healthy and productive years.
The 4th annual SER-CAT Symposium 16 March 2007, National Cancer Institute at Frederick, Frederick, MD, USA The 2007 Meeting of the American Crystallographic Associstion 21-26 July 2007, Salt Lake City, UT, USA The 9th International Conference on Biology and Synchrotron Radiation 13-17 August 2007, Manchester, England Item 1: January 2007 Publications by
Members: 1: Guan R, Mariuzza RA. Item 2: Tips and Tricks Wei Yang (NIDDK): Crystallization of Protein-DNA Complexes (updated)
Macromolecular interaction is essential, necessary and unavoidable in a living organism. Specific interactions among macromolecules are required for molecular machinery assembly and for progression and regulation of metabolic reactions. To fully understand a biological process, it is essential to determine the atomic structures of and interactions among components of a macromolecular complex and to decipher how these structures and interactions change during a reaction or signaling cycle. Some macromolecular complexes are naturally stable, for example tetrameric hemoglobin, nucleosome, and ribosome. But most macromolecular complexes are formed only transiently, e.g. an enzyme and substrate complex, a growth factor and its receptor interaction, or transcription factors assembled on a promoter. To determine structures of macromolecular complexes, whether stable or transient, has become a common practice of structural biologists in the 21st century. (Full Article) Xinhua Ji (NCI):Lysine Methylation It appears that lysine methylation should be considered a routine step not only in traditional (low-throughput) crystallization trials but also for structural genomics (high-throughput) attempts. Walter and co-workers outlined a detailed protocol with ten examples in their recent article (Structure 14:1617-1622, 2006). The protocol was derived from previously published method by Rayment and co-workers (Science 261:50-58, 1993) and Rayment (Methods Enzymol. 276:171-179, 1997). A recent success within the NIH X-ray Diffraction Group was reported by Schubot and Waugh (Acta Cryst. D60:1981-1986, 2004), showing that the method was pivotal in the de novo crystallization of a ternary complex that contains three protein molecules! Click for Introduction and tips and tricks in Crystallization, Post-crystallization treatments, Derivatization, Diffraction, Symmetry, Structure Solution, Structure Refinement, and Structure Analysis.
Item 3: Topic Discussion Click for previous discussions on: Low Resolution Crystallography, PHASER, HKL2000, Parallel Protein Expression, Structural Genomics, NCS, Missing Atoms, Trends in Crystallography, and Absorption Correction.
Item 4: Dr. Zbigniew Dauter's Lectures at the NIH (03/29-31/2005) |
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