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Protein
Crystallography Newsletter
Volume 1, No. 6, July 2009
In
this issue:
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Continuing
Education Webinar
Caveat
Emptor: What is the
Right X-ray Source for You?
Presenter: Joseph D. Ferrara, Ph.D.
August 26th at 11:00 AM EDT
(15:00 GMT)
Click
here to register |
New
CrystalMation™ Intelli-Plate™ 96-3 well crystallization
plate that is optically clear, UV-transmissible, with low
birefringence properties.
Reference
Tables
Resolution vs. Crystal-to-Detector Distance
 
Resolution as
a function of crystal-to-detector distance for CCD
(left) and IP
(right). Click to enlarge.
Remarkable
Creatures: Epic Adventures in the Search
for the Origin of Species by Sean B. Carroll.
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Crystallography
in the news
July
23, 2009. Rice University researchers have used X-ray
crystallography to solve the structure of the shell of the hepatitis
E virus.
July 17, 2009. Prof. Wladek Minor, and his research team at
the University of Virginia Health System within the Midwest
Center for Structural Genomics (MCSG), celebrate the deposit
of their thousandth
protein structure into the Protein Data Bank (PDB).
July 14, 2009. Prof. Andrzej Joachimiak and a team of
researchers at the U.S. Department of Energy's (DOE) Argonne
National Laboratory, in collaboration with scientists at the
University of Chicago, have determined the structure of a protein
crucial to the virulence of anthrax bacteria.
June 11, 2009. The Faculty of Health Sciences at the
University of Copenhagen has opened the doors of its new
research center, The Novo Nordisk Foundation Center for
Protein Research headed by director Michael Sundström.
Low
birefringence crystallization plate
Rigaku has just introduced the NEW
CrystalMation™ Intelli-Plate™ 96-3 well low-profile
crystallization plate designed for sitting drop vapor
diffusion crystallization experiments. The CrystalMation
Intelli-Plate is constructed from optically clear,
UV-transmissible, chemically resistant plastic with superior
low-birefringence. The low-profile construction allows for
higher density in plate storage and imaging systems,
maximizing your investment and valuable space. Designed to be
a substantial improvement in existing low-profile plates, the
new CrystalMation Intelli-Plate 96-3 allows for superior
sealing due to thicker well design and a flat sealing surface.
It has been built to the SBS (Society for Biomolecular
Screening) standard dimensions with 8 vertical reservoirs
versus 12 horizontal reservoirs and is compatible with
automated instrumentation including the CrystalMation line of
instruments from Rigaku.
Request a copy of the Intelli-Plate
96-3 product document.
What
is the right X-ray source for you?
Rigaku
Life Sciences Webinar Series continues on August 26th. In
the previous webinar in this series, we reviewed some of the
maintenance procedures associated with rotating anode X-ray
generators. Now we will explore the properties of X-ray sources, that is, the combination of
X-ray generator and X-ray optic. The discussion will cover properties such as focal spot
size, divergence, spectral purity, beam size and shape and how
they affect data quality. Upon completion you will have a
better understanding of what type of source best suits your
needs.
Click
here to register.
Useful
links for crystallography
Protein
Science - virtual issues are now available.
UCLA
Merohedral Twinning Server - twinning continues to plague
crystallographers. Luckily there are a number of useful
websites that offer assistance when encountering this problem.
Todd Yeates and Barry Fam maintain the UCLA Merohedral
Twinning Server as a service to the community. You can submit
a data set and test whether you have a perfect merohedral twin
or a partial merohedral twin.
Selected
recent crystallographic papers
Robust, high-throughput solution structural analyses by
small angle X-ray scattering (SAXS). G. Hura, A. Menon, M.
Hammel, R. Rambo, F. Poole, S. Tsutakawa, F. Jenney, S.
Classen, K. Frankel, R. Hopkins, S. Yang, J. Scott, B.
Dillard, M. Adams and J. Tainer. Nature
Methods Published online: 20 July (2009).
Mapping the structure and conformational movements of proteins
with transition metal ion FRET. J. Taraska, M. Puljung, N.
Olivier, G. Flynn and W. Zagotta. Nature
Methods 6, 532-537 (2009).
The Human SepSecS-tRNASec Complex Reveals the
Mechanism of Selenocysteine Formation. S. Palioura, R. Sherrer,
T. Steitz, D. Söll and M. Simonovic. Science 325,
No. 5938, 321-325 (2009).
G-protein-coupled receptor structures were not built in a day.
T. Blois and J. Bowie. Protein
Science 18, No. 7, 1335-1342 (2009).
Book
review:
Remarkable Creatures: Epic Adventures in the Search for
the Origin of Species
by Sean B. Carroll
I first heard about this book in an interview
with the author on Science Friday. I was intrigued and ordered
myself a copy the same day. The book is an elucidation of our
understanding of evolution. This book describes the three
categories of scientists involved in this process:
naturalists, paleontologists and molecular biologists. The
naturalists include Alexander von Humboldt, Charles Darwin,
Alfred Russel Wallace and Henry Walter Bates. These scientists
risked life and limb in pursuit of answers.
The paleontologists included Eugene Dubois, Roy Chapman
Andrews, Neil Shubin and the Leakeys. Dubois is the discoverer
of Java Man. Andrews began his career mopping floors at the
American Museum of Natural History and became director many
years later. Several character traits given to Indiana Jones
came from Andrews, including the six-shooter and the fear of
snakes. Shubin discovered the Tiktaalik, a sea-to-land
transitional species, in 2004. The Leakeys, of course, are
responsible for much our knowledge of early hominids and how
they used tools.
The last section covers the modern scientists who have helped
us understand evolution including, Linus Pauling, who really
needs no further introduction, and Allan Wilson. Wilson first
studied the genetics of chimpanzees and humans, and provided
the idea of a mitochondrial Eve. A great tribute to Charles
Darwin, the book celebrates the 200th anniversary of his birth
and 150th anniversary of the publication of The Origin of
Species.
Joseph D. Ferrara, Ph.D.
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