Dear Chang,
One need to set resolution cut off, to have a meaningful data without
losing high resolution data and keeping data integrity. Some key quality
indicators like I/Sigma I, CC 1/2 and Rpim etc., at outer most shell need
to be considered. What was the CC 1/2 value in outer shell ?
UCSF chimera or chimeraX versions both could do the alignment of multiple
structures that also pop up the sequence alignment with secondary
structures highlighted in different colors through Match Maker. Up-to six
structures I have aligned.
Best regards
Rajivgandhi Sundaram.
On Wed, Apr 8,
Any paper published should share the data publicly, it is the job of the
journal editor to ask so. If they don't want to disclose to scientific
community then, how one could trust the data published in that paper
describes active site and key structural information. Contact the editor of
the
This following screen Is generally used for DNA but one can give a try for
dna-protein complex as well.
https://hamptonresearch.com/product-Individual-Natrix-Natrix-2-Natrix-HT-Reagents-512.html
https://www.jenabioscience.com/crystallography-cryo-em/screening/crystal-screens/jbscreen-nuc-pro
Dear Dr.BR
There could be two possibilities, you could try to do titration of dimer
into monomer loaded in cell or vice versa, and with subtraction of heat of
dilution from protein-protein titration. These kind of molecular
interaction involving distinct oligomer units need be addressed by any
There are literature shown this kind of possiblity to have dimerization
via water mediated interactions. But look whether in solution also they
could form dimer or not. How to figure out it is not non specific, it is
physiological relevant.
Cheers
SR
On Fri, Sep 27, 2019, 5:04 PM Vijaykumar
Dear prem,
I am sharing my experience with needle crystal that worked for me.
1.First check that salt or a protein crystal by SDS PAGE or mass
spectroscopy.
2. For improvement of morphology and size, you could try microseeding of
your crushed crystal, generally needle crystal appear quickly,
Because MALS can capture distinct migrant form of the same protein,
sometimes protein with disorder and elongated structure behave differently
in SEC. In SEC we can't distinguish them. Whereas MALS have scattering at
three different angles, by that we can captures those multiple forms of
the
