--
Vandana kukshal
1-877-225-2034
Regd. England 2177994, VAT Reg. GB 480 7371 36
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Vandana kukshal
you
introduce me a server so that I can convert it to another PDB file starting
from 200 to 300?
Cheers,
Dialing
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Vandana kukshal
to getting your reply.
Cheers,
Dialing
--
Vandana kukshal
** **
Amit
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Vandana kukshal
but it was diffracted only 4 A.
The conditions of crystallization recipes are 4.5% PEG 1000, 0.1M Tris and
25mM Na citrate. I really need your suggestions regarding how can i
improve my diffraction quality?
Your support is highly appreciable.
Best Regards
AFSHAN
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Vandana kukshal
? Any suggestion about this super ice rings?
Thanks!
Tiantian
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Shanghai Institute of Materia Medica, Chinese Academy of Sciences
Address: Room 101, 646 Songtao Road, Zhangjiang Hi-Tech Park,
Shanghai, 201203
--
Vandana kukshal
--
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center For Genetic Engineering and Biotechnolgy
India
chain
atom is this wil be correct way to do these calculation. welcome ur
valuable sugessions .
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center For Genetic Engineering and Biotechnolgy
India
related
molecules for a given crystal structure. But I'm looking for some
program/software (for batch) by which I can find out the number
of symmetry related molecules (distance cutoff = 5A) interacting with
a given chain in a crystal structure.
Thanking you,
suku
NIBIO, Osaka
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Vandana
Fellow
The Radolf Laboratory
Department of Medicine
University of Connecticut Health Center
[w] http://spirocheteresearch.uchc.edu
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center For Genetic Engineering and Biotechnolgy
India
?
Best wishes
Xinghua Qin
--
Xinghua Qin
Room 4022, Center for Life Sciences,
China Agricultural University,
No.2, Yuan Ming Yuan West Road, Haidian District,
Beijing,China,100193
Tel: +86-10-62732672
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center
hello
if u are getting merged spot then try to increase detector distance it may
work . instead of this u try to reduce delta phi (gonimeter phi angle per
frame) default it is 1 degree u can try 0.5, 0.25 degree.
take it to synchrotron which is far away?
thanks
Careina
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center For Genetic Engineering and Biotechnolgy
Aruna Asaf Ali Marg
110 067 New Delhi
INDIA
to determine the sequence that can fold into a compact and stable 3D
domain. What kinds of methods can we choose?
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Best regards,
XH Wu
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Best regards,
Xianhui
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center For Genetic Engineering and Biotechnolgy
instead
of Beta mercaptoethanol.
for one of my crystallization experiment i used 1- 10 mM of Beta
mercaptoethanol.
--
vandana kukshal
CSIR-senior research fellow
X ray lab ,MSB division
central drug research institute
lucknow
--
Vandana Kukshal
Postdoc Fellow
structure biology group
hello sir ,
recently i have collected one data of 3.0 A of a
protein having no sequence homology with any known PDB .
but
while fold prediction i got 100 % identical fold with some of the
protein .
space group of my protein is P622 and showing 6 molecule
in a assymetric unit.
the
how to make covalent
bond between ligand and protein residue by using CCp4 package
i have one Query .
after using phenix auto build for building model R factor and R free
reduced but B factor is increesed for all the atom .what next i should do
to decrease the B factor of atoms.
hello
this is not a new question i was searching this in archives but i
did'nt get .
just send me link for this .
i want to link AMP covalently with lysine in my structure (phosphoamide
bond)how i will do this in coot and refmac .
in turbo there is option make bond but in this
i have one query. that if we have a multi domain protein structure to
solve ,and we know about only one small domain of the protein for MR .
other domain structure is not known then how we can proceed.
is there any procedure to utilize phase from the solution with known
domain .
hello
i have 3.25 A data of multidomain protein with 4 individual domain
.one domains structure is already known . and for others domain 40 %
simmilar structure is known . when i am running phaser with one known
domain i am getting the solution but after getting solution i
hi
i am solving one structure
in which after refinement i got R factor=27
and R free =27.7
i want to know that is it correct or i did some over refinment
the Resolution is 3.0 A
i am using restrain refmac for refine ment and coot for fiting
its resolution range is 116.248 -3.00
number of used reflections 20215
the R factor is 27.7
and R free is 27.0
and if i am doing further restrain refinement with 0.03 geometry weight
R factor is going down to 25.5
but R
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