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Newsletter 140 January 29, 2007 |
The
NIH X-Ray Diffraction
Interest Group
Newsletter
web site: http://mcl1.ncifcrf.gov/nihxray
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The 4th annual SER-CAT Symposium 16 March 2007, National Cancer Institute at Frederick, Frederick, MD, USA Dear Colleagues, The response to the first mailing of the information regarding the SER-CAT
meeting on March 16th has been very limited, with only a few participants
registering. It will be difficult to create a program without knowing ahead of
time who would like to present. The meeting should be very interesting, with the
plenary lecture to be delivered by Cynthia Wolberger (HHMI/Hopkins).
I would like to urge everybody interested in participation, and
particularly in giving a talk, to register as soon as possible. Please note that
the registration fee of $50 will be charged each participant in order to pay for
all three meals on the day of the meeting. More details can be found on the web
page: http://mcl1.ncifcrf.gov/sercat/
Again, please register as soon as possible.
Alex Wlodawer
9th International Conference on Biology and Synchrotron Radiation 13-17 August 2007, Manchester, England Item 1: December 2006 Publications by
Members: 1: Lee JY, Yang W. 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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This site is maintained by Dr. Xinhua Ji (jix@ncifcrf.gov) on the NCI-CCR-MCL server (http://mcl1.ncifcrf.gov). |