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Crystallography in the news
February 13, 2009. Diamond team unveil
the structure of a biological protein
from the vaccinia virus at the American Association for the Advancement of
Science meeting in Chicago—an important step in developing new therapies to
treat viruses.
February 10, 2009. Long-sought protein
structure may help reveal how the "Gene Switch" works. The biochemical
puzzle surrounding the switch is the mechanism by which the protein binds cAMP
at one end, then attaches to and activates a gene (DNA) at the other end.
January 21, 2009. New Jersey-based
biotechnology start-up company Nexomics Biosciences is to apply cutting edge
platform technologies based on large scale protein production, Nuclear Magnetic
Resonance (NMR), and X-ray crystallography in drug discovery efforts.
The
ultimate homelab optic for small crystals?
High-throughput crystallization methodologies
often result in smaller crystals. In addition, new research is increasingly
focused on proteins that form crystals with longer unit cell lengths. VariMax™
optics were designed with the performance and flexibility to meet both of these
twin challenges by providing either exceptional spatial resolution or very high
flux depending on the sample and experimental design.
The new Rigaku VariMax VHF represents the
pinnacle of current X-ray optics engineering for today's smaller protein
crystals. It delivers a 100 μm (FWHM) beam in which the divergence can be
easily adjusted in software to optimize performance for any unit cell length.
Optimization of the X-ray beam is accomplished
using a motorized, patented adjustable slit assembly that sets the beam
divergence. The VariMax VHF optic is capable of delivering very high flux when
working with systems requiring moderate resolving power and high speed data
collection. When greater peak separation is needed, it is readily available with
a lower beam divergence and some attenuation of flux.
Request a copy of the VariMax brochure.
Protein
crystallography webinar series
The new Rigaku Life Sciences Webinar Series begins in March with a course on
cryo-crystallography. These free instructional lectures are designed to provide
continuing education in protein crystallography methods. Each webinar in the
series will tackle a new topic ranging from optimization of crystallization
conditions to SAD phasing.
Selected recent crystallographic papers
X-ray structure of native
scorpion toxin BmBKTx1 by racemic protein crystallography using direct methods.
K. Mandal, B.L. Pentelute, V. Tereshko, A.A. Kossiakoff and S.B. Kent. J
Am Chem Soc. 131(4), 1362-3 (2009).
X-ray imaging: Caught in a spin. Keith A. Nugent. Nature
Physics, 5, 17-18 (2009). An algorithm that enables a
protein's molecular structure to be determined from the faintest of diffraction
patterns could increase the potential of next-generation X-ray sources.
Molecular Mechanisms of HipA-Mediated Multidrug Tolerance and Its Neutralization
by HipB. Maria A. Schumacher, Kevin M. Piro, Weijun Xu, Sonja Hansen, Kim Lewis
and Richard G. Brennan. Science, 323,
396-401 (2009).
FAQ: How to cryo-protect and mount crystals
Diffraction data collection at cryogenic
temperatures, from flash-cooled protein crystals, has become a routine part of
protein crystallography. In both the home laboratory environment, and at the
synchrotron, the benefits of low-temperature data collection are such that room
temperature work is now a rarity. An understanding of best practices that have
been refined over the years is essential for acquiring high quality data sets so
as to refine maximum resolution structures.
These best practices have been distilled into a
easy-to-follow pamphlet as part of Rigaku's Techniques in Cryocrystallography
Series. The document, Cryoprotecting & Mounting Crystals, covers all
aspects of the procedure—from the application of cryoprotectant, to crystal
and loop wafting, and then dewar to goniometer transfer. Please share this
document with colleagues and students.
Download
the cryo document and/or register
for the cryo webinar.
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