Re: [ccp4bb] Exciting postdoctoral position in protein complexes operating in human DNA replication by CryoEM in Leicester

[PiscoScience]

El El jue, 24 de sep. de 2020 a la(s) 11:48, Videler, Tennie (Dr.) <
h...@leicester.ac.uk> escribió:

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> *Apologies for cross-posting*​
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> Dear all,
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> we are looking for highly
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> motivated candidates to apply for a 2-year postdoctoral position funded by
> a collaborative grant from the King Abdullah University of Science and
> Technology (KAUST). The project investigates the structure and function of
> key protein complexes operating in
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> human DNA replication using cryo-Electron Microscopy (cryo-EM). The
> successful candidate will join a vibrant community of structural biologists
> in the Leicester Institute for Structural and Chemical Biology (LISCB), and
> will be based in the research group
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> of Dr Alfredo De Biasio.For
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> more information about his research please visit the lab website:
> https://le.ac.uk/liscb/research-groups/alfredo-de-biasio
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> For this project, the De Biasio group collaborates
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> with the KAUST laboratory led by Prof. Samir Hamdan, a leading expert in
> the biochemistry and single-molecule analysis of human DNA replication.
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> The Leicester Institute for Structural and Chemical Biology (LISCB) is a
> centre of research excellence initiated by the University
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> of Leicester. Aided by >£4m in investments in both equipment and new
> appointments, the research within LISCB targets fundamental questions in
> molecular biology through integrated structural approaches. Importantly,
> the LISCB is the heart of the new Midlands
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> cryo-EM consortium and hosts a fully operational 300kV Titan Krios
> electron microscope with K3 and Falcon 3EC direct electron detectors and
> associated high-performance computational infrastructure.You'd
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> get to work with Drs Christos Savva and TJ Ragan as well as with Alfredo
> and his group.
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> Advert:
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> https://jobs.le.ac.uk/vacancies/2232/postdoctoral-research-associate.html
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> Postdoctoral Research Associate - University of Leicester
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> Highly motivated candidates are invited to apply for a 2-year postdoctoral
> position funded by a collaborative grant from the King Abdullah University
> of Science and Technology (KAUST). The project investigates the structure
> and function of key protein complexes
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> operating in human DNA replication using cryo-Electron Microscopy
> (cryo-EM).
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> jobs.le.ac.uk
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> *Deadline is 20 October*
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> Any questions please contact Alfredo on ad...@leicester.ac.uk
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> kind regards,
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> Tennie
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> Dr Tennie Videler
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> LISCB manager
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> Leicester Institute of Structural and Chemical Biology
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> Office 025 Henry Wellcome Building
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> University of LeicesterLE1
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> 7HB
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> for now: 07850-996863
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> --
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>



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Re: [ccp4bb] tetrameric tag for extracellular proteins

[Srivastava, Dhiraj]

P53 tetramerization domain might be a way to go.


From: CCP4 bulletin board  on behalf of Comolettis 
<85822939...@gmail.com>
Sent: Friday, September 25, 2020 9:59 PM
To: CCP4BB@JISCMAIL.AC.UK 
Subject: [ccp4bb] tetrameric tag for extracellular proteins

Hi all,

Following what someone recently suggested, Fc tag is a great way to dimerize a 
secreted protein. I have successfully tried the TNF receptor-associated factor 
1 tail to trimerize and the COMP (cartilage oligomeric matrix protein) to 
pentamerize my monomer but I can't identify a suitable tag to tetramerize my 
construct.
Any pointer?

Thanks,
Davide Comoletti
VUW, Wellington, NZ



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[ccp4bb] AW: Re: [ccp4bb] short anti-parallel homodimerization motifs

[Hughes, Jonathan]

Hey Yong,
Oooh, thank you - and what's more, the crystals are sapphire blue (but it's the 
protein that does it, not us!).
The dimer affinity is not high, even with the rest of the protein included and 
we have never studied  the long helix alone, so it might not anti-parallel 
dimerize at all. On the other hand, it has two somewhat flexible positions, so 
in the free state it might be able to find a different energy minimum.
Good luck!
Jon

--
Jon Hughes
Sent without the use of Apple products.


 Yong Tang schrieb 

What a beautiful structure, Prof. Hughes - perfect crystallographic dimeric 
symmetry! Harder to dissect and isolate the dimerization element to my first 
look but I will look closer. yours, -yong

On Thu, Sep 24, 2020 at 5:07 PM Yong Tang 
mailto:liutan...@gmail.com>> wrote:
Thanks so much Jon - let me look into it. Yours, Yong

On Sep 24, 2020, at 4:59 PM, Hughes, Jonathan 
mailto:jon.hug...@bot3.bio.uni-giessen.de>> 
wrote:


hallo yong,
the 60 Å connecting helices in 2VEA (Cph1 phytochrome) form a non-physiological 
antiparallel dimer (at least with the help of the attached domains)
best
jon

--
Professor Jon Hughes,
Plant Physiology,
Justus Liebig University, Gießen, Germany.
email: jon.hug...@uni-giessen.de
homepage: http://www.uni-giessen.de/fbz/fb08/Inst/pflphys
Sent without the use of Apple products



Von: CCP4 bulletin board mailto:CCP4BB@JISCMAIL.AC.UK>> 
Im Auftrag von Yong Tang
Gesendet: Donnerstag, 24. September 2020 21:19
An: CCP4BB@JISCMAIL.AC.UK
Betreff: [ccp4bb] short anti-parallel homodimerization motifs

Dear all,

I'm wondering if you have personal experiences with an antiparallel 
homodimerization motif that I may use to add to my target protein for 
homodimerization. I was thinking along the lines of a helix or beta sheet (or 
hairpin) that is capable of antiparallel homodimerization.

For the interest of minimizing the size of such a "fusion" or "tag", a 
"full-size" dimerization domain is less favorable.

Thank you in advance for your tips. Sincerely, -yong



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