To any interested job seekers:
Please see below the description for a Research Associate position open in the
Protein Purification/X-ray Crystallography department at the New York
Structural Biology Center. This is a permanent, full-time position suitable for
a Master's degree holder.
Inquirie
Dear Colleagues,
I would like to draw your attention to a job opening here in Berkeley
California, for a Cryo-EM Facility Manager:
https://lbl.referrals.selectminds.com/jobs/cryo-em-facility-manager-3801
This position requires expertise in biological cryo electron microscopy
(cryo-EM)
Dear Colleagues,
H3 Biomedicine is at the forefront of cancer genomics and drug discovery (
www.h3biomedicine.com). Structural biology plays a prominent role in
underpinning our mechanistic understanding of disease biology and
empowering our drug design.
We have an exciting opportunity for a pos
Hi Deepak,
If this is a metalloprotein, include higher concentration of the metal in
the crystallization drop. It may act as a glue in the interfaces and give
you a good crystal.
Jackie Vitali
Cleveland State University
On Tue, May 18, 2021 at 6:20 AM Deepak Deepak
wrote:
> Dear all,
>
> I ha
Scientific Web Application Developer (RCSB/PDB Rutgers)
Summary
We are looking for a full-stack developer with a minimum of five years experience using modern database and web technologies. The
candidate should enjoy engaging with other developers and scientists in a collaborative team environm
Dear Colleagues,
I am writing to let you know that AbbVie’s Cystic Fibrosis Biology Group is
currently looking for a Post-doctoral researcher to study structural and
functional properties of Cystic Fibrosis Transmembrane Receptor (CFTR)
protein using Cryo-EM and cellular functional assays. The goa
If the foldamer(s) have exposed flexible parts they may impede ordered
crystallisation. Perhaps some minor tweaks to the foldamer or foldamers you are
co-crystallising with might lead to a better crystal contacts?
For example removing one or a few residues from the end(s) or shortening a loop.
M
Dear Deepak,
As some will have already said a good first check is to X-ray the crystals at
the temperature they were grown at. This is not too hard and there are numerous
approaches available. Some synchrotron sources, e.g. SSRL, have even enabled
this as a remote capability. This can tell you
Herman's suggestion is very good. But I'd go one step further and try to grow
crystals in 30-40% PEG400. Then you definitely do not need any additional
cryoprotectant. There is a chance that your crystals are of poor quality to
start with. In that case no cryoprotection will help. You can test
Hi all,
due to a cancellation we still have one open position in my group within
the DFG-funded graduate school MiCon.
Look at the website for further information (and don't worry about the
deadline issue)
https://www.ruhr-uni-bochum.de/micon/positions/index.html.en
Please get in touch if yo
Dear Deepak,
the cryoprotection may destroy the diffraction. I would also try diffraction at
room temperature, using special sleeves to prevent dehydration. With 20%
PEG400, you could also try to freeze the crystals without using additional
cryoprotectant. If you are lucky, it may work.
Best,
H
Dear Deepak,
I have a few suggestions:
1) First you can send it to synchrotrons, particularly microfocus beamlines
and shoot as many good in-house diffracting crystals.
2) Setting up crystallisation by micro batch method under Al's oil at
various vapour exchange rate may help. But
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