Newsletter 138
January 1, 2007


The NIH X-Ray Diffraction Interest Group

Newsletter web site: http://mcl1.ncifcrf.gov/nihxray

Happy New Year!
    

Advances in Protein Crystallography 24 - 25 January 2007, South San Francisco, CA, USA

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. 
 UvrD Helicase Unwinds DNA One Base Pair at a Time by a Two-Part Power Stroke.
Cell. 2006 Dec 29;127(7):1349-60. PMID: 17190599
  
2:  Yang W. 
 Human MutLalpha: The jack of all trades in MMR is also an endonuclease.
DNA Repair (Amst). 2006 Dec 1; [Epub ahead of print] PMID: 17142111
   
3:  Wang J, Dauter M, Dauter Z. 
 What can be done with a good crystal and an accurate beamline?
Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1475-83. PMID: 17139083
   
4:  Weston MC, Schuck P, Ghosal A, Rosenmund C, Mayer ML. 
 Conformational restriction blocks glutamate receptor desensitization.
Nat Struct Mol Biol. 2006 Dec;13(12):1120-7. PMID: 17115050

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)

Part 1: "How to read international tables?"

Part 2: "Data collection strategy" and "Twinning"

           "Phasing methods - a general introduction to all methods"

Part 3: "SAD phasing, Quick halide soaking, and Radiation damage 

           with possible use of it for phasing"
This site is maintained by Dr. Xinhua Ji (jix@ncifcrf.gov) on the NCI-CCR-MCL server (http://mcl1.ncifcrf.gov).