See http://www.douglas.co.uk/PDB_data.htm, section 4
On 19 July 2012 20:58, james09 pruza wrote:
> Dear Crystallographers,
> Is there any rule of thumb for Protein concentration and molecular weight
> for crystallization trials of a soluble protein? Looking for high molecular
> wt. protein ~50
A position is available in the Centre for Translational Therapeutics (CTT)
within the College of Medicine, Biological Sciences and Psychology for a
talented postdoctoral structural biologist to work on a collaborative in-house
structural biology projects, with an emphasis on structure-based drug
Dear all,
I'm looking for some advices on the choice of some spectroscopic equipment for
our lab.
What we would like to have is the possibility of measuring Circular Dichroism
spectra, and perform kinetic analysis in fluorescence, possibly also with a
stopped-flow set up, for pre-steady state
Hi Sebastiano,
We have a Chirascan instrument with all the attachments (fluorescence, stopped
flow, multi-cell attachment, etc). It is by far the best CD
instrument that I have used. I have experience in the past with Aviv, Jasco,
and Olis instruments.
Cheers,
Scott
***
Asp is not a strong nucleophile, and coordination to zinc will make it less
so. It is more likely that a zinc-bound water is acting as a nucleophile.
If there is no observed water attached to your Zn, consider the possibility
of ligand-water exchange, as in bacterial beta-carbonic anhydrases.
Roge
Dear all,
The EDS server was unfortunately down for a number of days. However, as of
yesterday it is up and running again. Apologies for the inconvenience.
http://eds.bmc.uu.se/
--Gerard
**
Number of years ago Jaru Jancarik (the author of Screen I & II sold by HR)
while in Berkeley Structural Genomics Center (or may be even earlier) made an
observation regarding protein precipitation in condition A6 in that very
screen. Based on this observation HR sells now PCT (protein concentrat
Noor,
Thank you very much for your inquiry. As we all know, thermodynamic principles
of cooperativity and allostery have long been used as a foundation to begin
understanding the complex interplay between associated ligand binding events.
In principle, the delta Tm shifts that occur when multi
Hi All,
I was collecting some data at home on a crystal from a protein containing a
ferredoxin domain. This crystal was originally red-brown in colour, but after
16h of data collection, a large portion of it appears not be colourless. The
crystal still seems to diffract fine (beyond 2A).
I assu
Actually with haeme, and or flavin containing enzymes it is known for the
cofactor to undergo reduction.
There is a recent JACS paper that explores these changes as a function of X-ray
exposure.
(2012) J.Am.Chem.Soc. 134: 2823-2834
Excellent work done in part at Allen Orville's X6A
As far as qual
Iron sulfur proteins tend to absorb less (although not zero) in the visible
when reduced. We see this with succinate dehydrogenase when we reduce with
dithionite to see the heme spectrum- the difference extinction coefficient
at the beta "peak" is actually negative because the baseline absorbance
I have sent this same query to JASCO earlier and did not get a response. So
thought of posting it here.
*Can a JASCO 810 CD spec be used as a simple UV-Vis Spec?*
I did not have a faster Spectrophotometer and so went ahead using JASCO 810
for a absorbance based enzyme assay/kinetics @ a constant
I too am also studying the reaction mechanism of an enzyme, but my
chemistry/enzymatic biochemistry is rather weak after many years of non-use and
no review. Does anyone know just as a general rule which residues are the best
to worst nucleophiles?
Sorry if this seems rather presumptuous, just
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