Do you use any Dnase while purifying your protein?
if not try that and set up new drops to check again.
Sent from my iPhone
On 13.01.2014, at 21:02, Debasish Chattopadhyay wrote:
> We crystallized a protein at 4 and 22 deg C in different conditions:
>
> from ammonium sulfate in acetate buf
POSTDOCTORAL RESEARCH FELLOW
Department of Biochemistry, Medical College of Wisconsin
A postdoctoral position is immediately available in the laboratory of Dr.
Jung-Ja Kim at the Department of Biochemistry, Medical College of Wisconsin
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Usually the skin is precipitated protein when it comes into contact with air.
In this case, avoiding contact with air may be the only way to avoid the skin,
i.e. crystallise using a technique that is not vapour diffusion, but for
instance microbatch, microdialysis or free interface diffusion.
O
We crystallized a protein at 4 and 22 deg C in different conditions:
from ammonium sulfate in acetate buffer pH 5
and
PEG4000 in Hepes buffer at pH 7.5
In both cases the drops have a slimy skin (almost feels like DNA). We
therefore think that the skin is generated from the protein.
I am sure s
Message below forwarded at the request of the conference organizers.
> From: Dorit Hanein
> Subject: [3dem] Reminder - Cryo-EM 3D Image Analysis Symposium 2014 - early
> registration ends Jan 31, 2014
> Date: January 13, 2014 11:02:14 AM EST
> To: "<3...@ncmir.ucsd.edu>" <3...@ncmir.ucsd.edu>
>
Announcement: Standardization of Amino Acid Nomenclature
The wwPDB is transitioning to use the nomenclature for pyrrolysine and
selenocysteine as recommended by the joint nomenclature committee of
IUPAC/IUBMB.
Starting in January, PYL (for pyrrolysine) and SEC (for selenocysteine) will be
used
Specifically for fluorescence
does your ligand fluoresce?
It is possible if it has indol group or some aromatic organic compound
Does your protein has a tryptophan or tyrosines in the binding site?
If yes may be a fluorescence titration experiment could be the solution.
Also fluorescence
FRET， CD， Fluorescence， NMR chemical shift assay, isotope-labelled ligand
interaction assay, protein melting temperature assay, gel filtration retention
assay, gyration radius assay by Malls, native page gel analysis, etc.
Acoot
On Monday, 13 January 2014 8:51 PM, HJ Lee wrote:
Sorry for
Ho Jun Lee,
Have you thought about differential scanning fluorimetry (Thermofluor)? With
this biophysical technique you can characterize protein-ligand interactions and
screen a wide variety of ligands using minimal concentration of ligand and
protein. All you need is a quantitative PCR machine
Sorry for the off topic. I'm looking for a way to monitor
protein-(potential) ligand interaction. The ligand is small molecule
(mw~250) and we're looking for its potential interaction with couple human
proteins. (We do not know this small molecule interacts with these human
protein or not.)
Is the
"reverse translation" from protein to nucleotide does not yield a unique
sequence. Your best bet is to use the BLAST feature that searches your protein
sequence against the entire genbank DNA database translated into protein:
http://www.ncbi.nlm.nih.gov/BLAST/Blast.cgi?PROGRAM=tblastn&PAGE_TYPE=
-- Forwarded message --
From: Sumita Karan
Date: Mon, Jan 13, 2014 at 1:00 PM
Subject: DNA sequence from amino acid
To: CCP4BB@jiscmail.ac.uk
Dear all,
I am working on eukaryotic protein and have the amino acid sequence of the
protein but do no know the sequence of cloned gene.
D
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