Hi Tom,
Are your protein or related proteins known to dimerise?
Is the dimer perhaps the natural state, and are the high oligomers
non-specific aggregation?
That would be my first guess, knowing nothing about the protein you are
working on.
If you are absolutely certain that the protein should
Dear All,
After series of trial and even with the truncated forms, I find my protein has
the difficulty to contact to form the crystallization, or lacking the
nucleation center in the purified protein.
Will you please introduce the domains with witch my protein fused, there will
be more
Dear Timothy,
My is non-membrane protein. The proteins you recommended are also suitable,
right?
Cheera,
Acoot
On Thursday, 27 February 2014 7:07 PM, Timothy Craig tlmcra...@hotmail.com
wrote:
You may want to try cytochrome B 562 RIL (BRIL), T4 Lysozyme, rubredoxin, or
amicyanin.
Hi,
I'm sure this question has been addressed before and I
apologize for asking it again. I'm working on a protein
predicted to have multiple disulfide bonds. The protein is
expressed in an E. coli strain with an oxidizing cytoplasm,
and is purified under nonreducing conditions (no DTT, b-
I wouldn't worry about oxidation of SeMet; at least I never have. A number of
years back there was a paper published actually claiming that oxidised SeMet
has a higher and sharper absorption edge than reduced SeMet. Of course mixed
forms could complicate things but I would just purify like you
Hi Reza,
You have here an example of MAD data collected fromoxidized and
reducedselenomethionine-containing protein:
It states :phasing power of theoxidized data is doubled for the dispersive
signal and is 20% stronger
for theanomalous signal at the peak wavelength
Thomazeau K, Curien G,
Post Doctoral Positions in protein structure and function at the Karolinska
Institutet (Sweden)
Dear bulletin board,
A post-doctoral position (stipend, 1+1 year) is available at the Department of
Medical Biochemistry and Biophysics (MBB), Karolinska Institutet, Stockholm.
The project deals
Trying not to state the obvious but...HIV protease
-Original Message-
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Keller,
Jacob
Sent: Friday, 28 February 2014 8:43 a.m.
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Large Conformational Change Upon Binding
Another good example are nucleotide binding proteins - small GTPases
spring to mind, changing between GTP and GDP states and there are many
ATPases such as myosin to name only one of many, cheers, Matt.
On 2014-02-27 20:43, Keller, Jacob wrote:
Dear Crystallographers,
Does anyone know of
Hi all,
Any of you got some experience on purifying (and crystallizing)
VIL-rich proteins (actually, more particularly isoleucine rich). Tried
to purify my protein, but majority (if not all) of the proteins reside
in the inclusion bodies. Induction is at low temperature, overnight
and
Pheromone-binding proteins of lepidopteran moths (Antheraea polyphemus, Bombyx
mori, Amyelois transitella etc.). The C-terminal tetradecapeptide of these
proteins is a random coil in the ligand-bound form, and assumes a helical
structure in the absence of ligand which occupies the binding
Dear CCP4 Bulletin Board Members,
I am looking for Post-Doctoral candidates for a position in my laboratory
located in the University of Georgia's Department of Pharmaceutical
Biomedical Sciences. This position will assist in my ongoing NIH funded
infectious disease related projects that
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