.7% -15% 0.435 119774
>
> Note that I/SIGMA of each resolution shell is <2.5, so how should I do to
> process the dataset properly? Any suggestion about this super ice rings?
> Thanks!
>
> Tiantian
>
> --
> Shanghai Institute of Materia Medica, Chinese Academy of Sciences
> Address: Room 101, 646 Songtao Road, Zhangjiang Hi-Tech Park,
> Shanghai, 201203
>
--
Vandana kukshal
CP4BB@JISCMAIL.AC.UK
> Subject: [ccp4bb] How can improve diffraction quality
>
> Dear ccp4 user
>
> I am facing one crucial problem regarding diffraction. Actually the size of
> my crystal is good enough 0.5mm 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
>
--
Vandana kukshal
n?
>
> ** **
>
> Thanks in advance****
>
> ** **
>
> Amit
>
--
Vandana kukshal
troduce me a server so that I can convert it to another PDB file starting
> from 200 to 300?
>
> Cheers,
>
> Dialing
>
--
Vandana kukshal
reenshot?
>
> I am looking forward to getting your reply.
>
> Cheers,
>
> Dialing
>
--
Vandana kukshal
t;
>
>
>
>
> --
> patr...@douglas.co.ukDouglas Instruments Ltd.
> Douglas House, East Garston, Hungerford, Berkshire, RG17 7HD, UK
> Directors: Peter Baldock, Patrick Shaw Stewart
>
> http://www.douglas.co.uk
> Tel: 44 (0) 148-864-9090US toll-free 1-877-225-2034
> Regd. England 2177994, VAT Reg. GB 480 7371 36
>
>
--
Vandana kukshal
ral Biology Laboratory
> SLS, JNU,
> New Delhi-110067
>
--
Vandana kukshal
d TCEP in ur buffer 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 b
> > to have an idea of the intrinsically disordered regions in the protein,
>> transmemebrane regions and disulfide bonds that would certainly help you in
>> initiating in the right direction.
>> >
>> > Best wishes
>> > Gauri
>> >
>>
I 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
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.
better shape, did I got the point?
>
> 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
>
>
mit Luthra, Ph.D.
> Post-Doctoral 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
t;> The solution is getting clear in the room temperature within 5 mins when I
>> set up the trays.
>>
>> I would like to take any advice. I would appreciate your input.
>>
>> Best
>>
>> Min
>>
>
>
--
Vandana Kukshal
Postdoc Fellow
structure biology group
international Center For Genetic Engineering and Biotechnolgy
India
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
>
t;
> --
> Konstantin Korotkov, Ph.D.
>
> Research Scientist
> University of Washington
> Department of Biochemistry
> Box 357742
> Seattle, WA 98195-7742
>
> (206)616-4512
> k...@u.washington.edu
> --
--
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
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 n
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.
how to make covalent
bond between ligand and protein residue by using CCp4 package
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 homologous
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 f
total number of atoms are 5113
you can try glutathione and cysteine as reducing agent with conc
0.01-0.001M or higher
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 am
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 .
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