[ccp4bb] Crystallography Associate Position at Novartis

[Sprague, Elizabeth]

We have an opening for a Crystallography Research Associate position in the 
Structural Biophysics Group at Novartis (Cambridge, MA). The candidate must 
have a good foundation in protein expression  purification, and then 
crystallography and/or biophysics experience is desirable, but not required.

Please apply online with this link:
http://jobs.brassring.com/1033/ASP/TG/cim_jobdetail.asp?partnerid=13617siteid=5268Areq=144532BR

[ccp4bb] Disorder in crystal packing

[Paul Paukstelis]

Greetings,

Currently working on a DNA quadruplex structure in which 4 of the 10 
residues are partially disordered. 1.50 A resolution, and currently 
refined to R/Rfree of 12/14%. Apparent spacegroup is P4, two molecules 
in AU, both of which reside on the 4-fold to generate quadruplexes. 
Packing results in layers of quadruplexes that are perpendicular to the 
4-fold.  The issue is with the diordered residues that appear to mediate 
crystal contacts between these layers. There are some difference density 
planes that runs between the layers, and they are spaced 3.2 A apart, 
which would suggest nucleobase stacking, but there is no way to build 
into it.


Are there other examples of disordered (or most disordered) residues 
mediating crystal contacts in this way? I seem to recall some examples 
with partially disordered protein subunits/monomers being involved in 
packing. Other things to consider?


Thanks,

--paul

[ccp4bb] Crystallization of aggregation prone protein

[Debasish Kumar Ghosh]

Dear All,

I am working with a protein which is having an N-terminal unstructured region 
(approximate of length 40-60 amino acids) and C-terminal region which is having 
structured (possibly alpha helical region as probed by CD spectroscopy, 
Bioinformatic studies) property. The protein, in higher concentration (above 
2mg/ml), forms various oligomeric structure (probed by Atomic force microscopy) 
resembling annular type aggregation (may be called as protofibril). when using 
various deletion mutants lacking different regions of N-terminus and 
C-terminus, we found that the C-terminal 45 residues is responsible and 
sufficient to make this annular type aggregation (like seen in alpha Synuclein, 
though much bigger is size than alpha Synuclein annular oligomers). We tried 
with our best to crystallize both the full length protein and the C-terminal 45 
residues (which eventually has 37% sequence identity and 63% similarity [at 
Query coverage of 87%] with a putative UBA domain like structure of an archaeal 
protein). We tried various crystallization suites like PEG, PEG-II, Nucleix, pH 
clear etc to optimize the condition with no satisfaction at all.
So, it would be a great help for me if I can get advises so as to troubleshot 
this problem. All advises are deeply appreciated. 

Thank you,
Best regards,

Debasish Kumar Ghosh

CSIR- Junior Research Fellow (PhD Scholar)
C/o: Dr. Akash Ranjan
Computational and Functional Genomics Group
Centre for DNA Fingerprinting and Diagnostics
Hyderabad, INDIA

Email(s): dkgh...@cdfd.org.in, dgho...@gmail.com
Telephone: 0091-9088334375 (M), 0091-40-24749396 (Lab)
Lab URL: http://www.cdfd.org.in/labpages/computational_functional_genomics.html