Hi all,
I'm working on a protein structure which showed a special electrostatic
potential on its surface: positive on one end and negative on the other
end. I wonder to what extent I can say this pattern is determined by the
charged residues? If the residues are conserved, could I make a
Dear all,
I have a 2.4A structure(pdb code 3LAF)with an average protein b-factor of
48. I wonder whether it's acceptable. Is there a direct correlation of
b-factor and resolution?
The R and Rfree are 21.1% and 23.1%, respectively.
This structure has a very high solvent content, 75%. Does it
according to Axel
Brunger's article about that topic.
Cheers,
Tim
On 05/16/12 15:46, Qiang Chen wrote:
Dear all,
I have a 2.4A structure(pdb code 3LAF)with an average protein
b-factor of 48. I wonder whether it's acceptable. Is there a direct
correlation of b-factor and resolution? The R
There are two immediate openings for protein crystallographer position in
Harvard Medical School. One of the research projects is focused on the
structural and functional investigation of Wnt signaling pathway. The
project is the close collaborative efforts between Professor Xi Hes lab
at
There is an immediate opening for a protein crystallographer position in
Harvard Medical Schools Childrens Hospital. The research is focused on
the structural and functional investigation of Wnt signaling pathway. The
project is the close collaborative efforts between Professors Xi He and
structures, I think.
Artem
On Thu, Jan 12, 2012 at 10:03 AM, Qiang Chen
c...@red.dfci.harvard.eduwrote:
Hi,
I'm working on a multi-domain protein which uses three domains to form
homodimer, and the full-length structure is available. We have solved
the
structure of one binding domain
Hi,
I'm working on a multi-domain protein which uses three domains to form
homodimer, and the full-length structure is available. We have solved the
structure of one binding domain alone and found its homo-binding mode is
totally different from that of the full-length protein.
Do you know
Hi guys,
I'm working on a multi-domain protein which uses three domains to form
homodimer, and the full-length structure is available. We have solved the
structure of one binding domain alone and found its homo-binding mode is
totally different from that within the context of the full-length
Peking University, College of Life Sciences seeks to recruit dedicated
postdoctoral fellows to carry out structural and functional investigation
of cell surface receptors in nervous systems.
The successful candidates will focus his/her research on elucidation of
molecular mechanism with which
Dear all,
I'm refining a structure which has both N-linked and O-linked
glycosylation. I use Phenix to do the refinement. It works well for the
N-linked NAG. I defined the link as the following:
apply_cif_link {
data_link = NAG-ASN
residue_selection_1 = chain A and resname NAG
Dear all,
on behalf of Jia-huai Wang, I post this message. For inquiries please
contact Jia-huai at jw...@dfci.harvard.edu.
Postdoctoral fellow position in structural biology
Peking University, College of Life Sciences seeks to recruit dedicated
postdoctoral fellows to carry out structural
Hi all,
The data I am working on has a strong translation vector. The space group
is C2221 and resolution is 2.3 angstrom. There are two molecules per AU
with a pseudo-2-fold axis.
On the cumulative intensity distribution plot, the theor and obser curves
totally do not overlap. I did
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