News 2006
May 2006
The number of PDB deposition from Bl10 10.1 at SRS has reached number 20.
The average resolution is 1.85 A with an Rfactor and Rfree of 17.1 and
20.6 respectively. The average number of amino acids in asymmetry unit of a
protein structure is 600. The average LAG time is in months from the date of
data collection to pdb deposition is 5.
April 2006
2006 British Crystallographic Association Biological Structure Poster
prize
Mr. Hamed Helal, a graduate student of the Structural Chemistry Unit at the
University of Manchester, Chemistry Department has won the 2006 BCA poster prize
for his work which presented data collected on BL10 at SRS (CCLRC Daresbury).
The poster title was "Structural studies of alpha-thrombin". The collaboration partners were H.Hamed, J. Habbash, J. Raftery, J.R. Helliwell (University of Manchester), M.Spano and M. Blakeley (EMBL-ILL, Grenoble), M.Cianci (CCLRC - Daresbury) and J. Hubbard (GLAXO - SmithKline, Stevenage).
Left Picture: (left to right): Michele Cianci, Monika Spano, Helal Hamed and John Helliwell. Right Picture: BCA Biological Structure poster prize. The rock is called a Blue John Crystal (mineral) from a quarry in Sheffield.
March 2006
First front cover for work done on MAD 10.1 at the SRS.
In
a recent JMB paper (March 10th 2006, vol 356, 1152-1162) , we present data that
support the possibility that in a cellular environment with low availability of
free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its
interaction with the copper chaperone. We obtained atomic resolution crystal
structures (the highest is 1.07 Å, obtained using BL10.1) and biophysical data
for human SOD1 in three metallation states: Zn-Zn, Cu-Zn and `as-isolated’.
These data represent the first atomic resolution structures for human SOD1, the
first structure of a reduced SOD1, and the first structure of a fully
Zn-substituted SOD1 enzyme. The Zn-Zn SOD1 dimer appears to be as stable as the
native Cu-Zn protein and would avoid problems associated with aggregation of
apo-enzyme.
Human Cu-Zn superoxide dismutase (SOD1) protects cells from the effects of
oxidative stress. Single point mutations of SOD1 are linked to the familial form
of motor neuron disease, a fatal progressive neurodegenerative disorder for
which there is currently no cure. Several hypotheses for SOD1 mutant toxicity
involve the mis-metallation of the enzyme and our previous work has shown that
amyloid-like filaments can be formed from metal depleted wild-type protein (J.
Mol. Biol. 328, 887-891 2003).
This work was funded by the Motor Neuron Disease Association U.K. ( www.mndassociation.org )
Journal
of Molecular Biology, issue for March 10th, Vol 356 issue 5.
The full reference is:
Strange, R. W., Antonyuk, S., Hough, M. A., Doucette, P. A., Valentine, J. S.
& Hasnain, S. S. (2006). Variable metallation of human superoxide dismutase:
atomic
resolution crystal structures of Cu-Zn, Zn-Zn and As-isolated wild-type enzymes.
J. Mol. Biol. 356, 1152-1162
February 2006
New-look Mad10 website launched. We must all recognize the hard work of Ms. Barbara Runcie at Daresbury Lab. Our Web Guru.
