Newsletter 121 May 8, 2006 |
The
NIH X-Ray Diffraction
Interest Group
Newsletter
web site: http://mcl1.ncifcrf.gov/nihxray
The 36th Mid-Atlantic Macromolecular Crystallography Meeting The 2006 Meeting of the American Crystallographic Association
Item 1: April 2006 Publications by
Members: 2: Yao Y, Mayer ML. 3: Kostelansky MS, Sun J, Lee S, Kim J, Ghirlando R, Hierro A, Emr SD, Hurley
JH. 4: Yamamoto Y, Moore R, Hess HA, Guo GL, Gonzalez FJ, Korach KS, Maronpot RR,
Negishi M. 5: Nowotny M, Yang W. 6: Yang W, Lee JY, Nowotny M. 7: Prabakaran P, Gan J, Feng Y, Zhu Z, Choudhry V, Xiao X, Ji X, Dimitrov DS. 8: Morizono H, Cabrera-Luque J, Shi D, Gallegos R, Yamaguchi S, Yu X, Allewell
NM, Malamy MH, Tuchman M. 9: Raychaudhuri S, Im YJ, Hurley JH, Prinz WA. Item 2: Tips and Tricks Please share your tricks with members of the group. Click for Introduction and tips and tricks in Crystallization, Post-crystallization treatments for improving diffraction quality of protein crystals, Derivatization, Diffraction, Symmetry, Structure Solution, Structure Refinement, and Structure Analysis.
Item 3: Topic Discussion - Low Resolution Crystallography I recently had a visiting seminar
speaker in my office, and was describing some of the new structures in the lab
to him. I was excited at the time to have the structure of a biggish
multiprotein complex and another biggish full-length mammalian signaling
protein to show off. The resolution was low in both cases, but for the
biological questions being asked about how domains and subunits interacted, the
structures were still informative. My visitor commented that “Your lab seems to
have a real problem with resolution.” We
have had a recent run of low resolution structures, whether due to bad luck, an
increased focus on larger proteins and complexes, or both. Axel Brünger wrote a review suggesting that this is a larger trend, a renaissance in low resolution crystallography (Brünger, 2005). From a crystallographer’s point of view, it is never a good thing to be stuck with low resolution data. But from a structural biologist’s viewpoint, things look different. The holy grail of the field is an integrated picture of the cell in which structural information is available at every size scale in the cell from atomic resolution crystal structures through light microscopy of whole cells. Our cryo EM colleagues are hard at work improving the resolution of their methods in order to bridge the gap. Low resolution x-ray crystallography also has a big part to play in the chain of imaging techniques as we try to bridge the gap from atomic to cellular structure.
Three examples from my lab follow: ... (Click for the entire article) Click for previous discussions on: 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"
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