could this make acceptable pictures of protein crystals?
http://www.ubergizmo.com/2011/11/the-extreme-60x-100x-magnifying-microscope-for-your-iphone/
I imagine holding the phone stable might be difficult - and that crystals may
be too far away from the lens in some types of crystallisation
On Sun, Nov 06, 2011 at 05:35:29AM +, Ramanuj Banerjee wrote:
I used CAD for merging datasets during MIR. I faced the same problem. The
solution is: the datasets you are trying to merge should have different
labels i.e if dataset 1 has labels: F and SigF, dataset 2 should be F_d1 and
Hi Mark,
I'd rather hold the iPhone to the lense of your regular microscope instead.
Jürgen
..
Jürgen Bosch
Johns Hopkins Bloomberg School of Public Health
Department of Biochemistry Molecular Biology
Johns Hopkins Malaria Research Institute
615 North Wolfe Street, W8708
When we were working on PheRS we noticed that our protein preps (and
crystals) had shades of color: sometimes they were pinkish and sometimes
yellowish, or even blueish (and often colorless)!
We solved the structure eventually and found a new metal-binding
microdomain previously not found in these
I agree: light yellow (straw-yellow) proteins often indicate metal-binding -
it's typically iron III. Zn salts tend to be colourless, and the Mn-pink is
too pale to be visible at protein (mM) concentrations. This can be determined
by doing flame-spectroscopy, if you don't mind destroying your
Cobalt leaching of TALON resin perhaps ?
Should be more orange type of color, but it depends on the concentration.
In any event if you shoot those crystals run a scan to find out what metal is
bound and use it for phasing if you have access to a MAD line.
Jürgen
On Nov 6, 2011, at 9:56 AM,
Hi Brennan,
we did some time ago a kind of similar experiment, where
we used Xe and Kr to contour the channels within Photosystem II (see
Gabdulkhakov et al, Structure. 2009 Sep 9;17(9):1223-34 for the pressure,
wavelength and derivatization time values we used)
However before doing this we went
Dear all
I have a protein soaked in a coordination compound containing platinum. Due to
some reason, I do not get the anomalous data at 1.072 angstrom, only got a set
of data at 0.973 angstrom. I have solved the phase through molecular
replacement, and refined the model to Rfactor=0.2204,
Hi everyone
I have a protein that is extraordinarily stable at PH=3.0 or even 2.0.
I want to crystallize it in the low PH and compare the differences between the
crystals in regular PH and low PH.
I was wondering how people set up the boxes in low PH, as usual buffers are
mostly less acidic.
