Hi Thierry,
We have worked on a number of proteins where the oligomerisation
state differs from that found in solution. A recent example is a
project we worked on involving the HC fragment of tetanus toxin
(see Qazi et al., J Mol Biol. 2007 Jan 5;365(1):123-34) which
crystallises
as a monomer. T
hi thierry
we had a case where Spo0A in the phospho form was a dimer
in solution, and in the non-phospho form was a monomer. in the
crystal, we had monomers of the phospho form, and (domain-swapped)
dimers of the non-phospho form. turns out that the crystallisation
conditions affected the behavio
Dear all,
Thank you for all your kind replies.
Here is a little bit more about the enzyme and how I carry out the assay at the
first place.
My enzyme is a lipid desaturase, originally from plant but overexpressed in
bacteria. FAD serves as a co-factor for this enzyme, in which FAD is reduced t
Mike:
It seems FAD is readily dissociable for your protein.Then, trust me, you
got to do it anaerobically in order to see the 450nm decrease upon reduction of
the enzyme by the substrate(better use excess substrate).
Sincerely,
Hongnan Cao
UCR
Date: Tue, 2 Dec 2008 11:11:53 -0800F
Hi Michael,
Fraser et al writes that in case of Synechococcus phytoene desaturase
'NAD+ and NADP+ were observed to be involved, whilst FAD was an
ineffective electron acceptor '
Biochem J. 1993 May 1;291 ( Pt 3):687-92
HTH
Guenter
PS The enzyme itself has no flavin bound?
michael nelson wro
Does the FAD actually dissociate on each turnover, or does it remain bound
and transfer electrons to an acceptor? Succinate dehydrogenase is an
example of the latter, and it can be readily assayed using a mediater
phenazine methosulfate to accept the electrons and transfer them to
a redox dye dich
Dear All,
I am trying to mutate a single amino acid in a PDB to see if the mutant
disturbs ligand binding. Does anyone know any software that can do such work?
Thanks a lot!
Macromolecular Machines involved in Translation and mRNA Transport
Post-doctoral positions are available immediately in the group of
Christine Dunham at Emory University School of Medicine. We are
interested in two separate but related projects: 1) the structure and
function of RNA and RNA-
Pymol
the question is, into how much trouble do you want to get ?
MD simulations ? Energy minimisation ? Then you will need to do more
than just mutate on the sreen one residue with Pymol.
Jürgen
On 2 Dec 2008, at 17:29, Hongmin Zhang wrote:
Dear All,
I am trying to mutate a single amino
Yes, it is better to have MD or energy minimization. Otherwise, with only
view on the screen, we can't tell if the mutated residue would disturb
ligand binding because of the side chain flexibility.
Best!
Hongmin
On Wed, Dec 3, 2008 at 12:50 PM, Juergen Bosch <[EMAIL PROTECTED]>wrote:
> Pymol
> t
In that case you might want to use CNS with model_anneal.inp or
model_minimize.inp, or the equivalents in phenix
Jürgen
On 2 Dec 2008, at 21:29, Hongmin Zhang wrote:
Yes, it is better to have MD or energy minimization. Otherwise, with
only view on the screen, we can't tell if the mutated re
Thanks! I think we still can't tell if the mutant would disturb ligand
binding or not.
Best!
Hongmin
On Wed, Dec 3, 2008 at 2:15 PM, Juergen Bosch <[EMAIL PROTECTED]>wrote:
> In that case you might want to use CNS with model_anneal.inp or
> model_minimize.inp, or the equivalents in phenix
> Jürge
Dear all,
I have a 3 A structure refined with REFMAC which gives consistently
average atomic B-factors of 40 A2, whereas the B factor from a Wilson
plot is about 60 A2. Is there any explanation for such a discrepancy?
There are no obvious problems:
No twinning, spacegroup P21 with two molecule
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