Dear All,
Will you please let me know what is the solvent-flattened electron density map
and how to get it?
Cheers,
Acoot
Dear All,
Suppose I have a crystal hit from the protein-metal complex, with the
possibility of that the hit is a salt crystal. When I diffract it by X-ray, I
got some metal (or salt) diffraction without the protein diffraction (maybe due
to too low protein resolution). Will you please tell
Dear All,
When I purified my protein by ion exchange chromatography for crystallization,
there were several peaks containing the target protein as analyzed by SDS-PAGE.
All these peaks have the same MW as determined by gel filtration coupled MALLS.
For crystallization purpose, can I merge
Dear All,
I am optimizing a crystal. In one of the optimizing conditions I find the
crystal is cubic-like shape (the crystal is not large, but absolutely not the
traditional tiny crystal. The crystal has some kind of faces and edges but
not so sharp, and it is absolutely not round). But after
Dear All,
For the question, I think for a protein-DNA interaction, the protein may
interact with any sequences of DNA, which will give a lot of combination of
protein-DNA sequence for crystallization screening. Or do anyone regard to
just try the crystallization of the protein-one specific
Dear All,
I am now working on the crystallization of a complex of protein-16 bp DNA by
co-crystallization. In the screening very small needle-like crystal occurs. If
not salt crystal, is there a method to know it is not the crystal of the DNA?
Cheers,
Acoot
FRET， CD， Fluorescence， NMR chemical shift assay, isotope-labelled ligand
interaction assay, protein melting temperature assay, gel filtration retention
assay, gyration radius assay by Malls, native page gel analysis, etc.
Acoot
On Monday, 13 January 2014 8:51 PM, HJ Lee
''Signals in the region from 250-270 nm are attributable to phenylalanine
residues,
signals from 270-290 nm are attributable to tyrosine, and those from 280-300 nm
are attributable to tryptophan. Disulfide bonds give rise to broad weak
signals throughout the near-UV spectrum.
''
I don't think it possible for protein purification purpose. There would be no
linear correlation between A280 and the protein concentration.
For pure protein analysis, as for minor amount protein used, it is possible.
Acoot
From: Karel Chaz
Dear All,
After series of trial and even with the truncated forms, I find my protein has
the difficulty to contact to form the crystallization, or lacking the
nucleation center in the purified protein.
Will you please introduce the domains with witch my protein fused, there will
be more
Dear Timothy,
My is non-membrane protein. The proteins you recommended are also suitable,
right?
Cheera,
Acoot
On Thursday, 27 February 2014 7:07 PM, Timothy Craig tlmcra...@hotmail.com
wrote:
You may want to try cytochrome B 562 RIL (BRIL), T4 Lysozyme, rubredoxin, or
amicyanin.
Dear All,
In the crystallography paper table 1, there is Values in parentheses are for
the highest resolution shell. Is this highest resolution shell same as the
OuterShell for the analysis result got by Scala?
I am looking forward to getting your reply.
Cheers,
Acoot
Ion exchange chromatography, this is the published method.
Acoot
From: Xinghua Qin xinghua...@126.com
To: CCP4BB@JISCMAIL.AC.UK
Sent: Monday, 4 June 2012 2:51 PM
Subject: [ccp4bb] How to know if ADP exists in the ATP-binding site of
bacterial expressed proteins
Deer CCP4ers,
How to know
Dear All,
I want to use dash line to present the salt bridge in a crystal structure in
the paper publication, for example the salt bridge formed between Glu (OE1 and
OE2) and Lys (terminal N).
Do you suggest I only draw a single dashed line between the terminal N of the
Lys and the closer
Dear All,
A lot of 3-D crystal structures highlight the salt bridges in the structure,
although some structures of them are got at high salt concentrations.
Will you please explain to me why the protein salt bridge can still exist in
the high salt concentration as used in the crystallization
Dear All,
A protein crystal can be got at pH 5 or 8, or a pH with much extreme value.
What will be the relatively extreme pH value to get the crystal on the protein
structure solved based on the crystal got? I mean usually we regard the
physiological pH as 7. If a crystal was got at pH 5, the
Dear All,
For the protein buffer for the crystallization purpose, if we buy from
Sigma-Aldrich, which types of NaCl and Tris are much suitable?
I am looking forward to getting your reply.
Cheers,
Acoot
Dear All,
Will you please give a comment on how the temperature influences on the
possibility to get protein crystal, and how the temperatures used to get the
protein crystals of the same protein influences the protein 3-D structures of
the same protein got based on the crystals of the same
http://www.oborges.com/rxpou/sglkxqkvddy.yflv
Acoot Brett
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