Hi,
If you have the correct solution, clashes may be due to loops. It may be
an idea to clip these off for the molecular replacement calculations
(loops might be shorter in the structure-to-be-solved than in the search
model, they may have different conformations in the
Hi,
I think this practice (requesting the data) is getting more and more
common these days with some scientists having published fake
structures. You are far more protected from scientific misconduct when
you provide the data to referees (this takes place through an editorial
system - you
I'd google for Bart Hazes and SSBOND myself. There is (or was) a server,
and the publication is Prot. Eng. 1988, 119, 25 (PMID 3244694). The server
seems to be down or has moved.
HTH, Fred.
Message du 04/03/12 05:07
De : Naveed A Nadvi
A : CCP4BB@JISCMAIL.AC.UK
Copie à :
Objet :
Hi,
You could try to lower the threshold used to contour the maps for these
side-chains (middle mouse button if you have a 3 button mouse with a
wheel in the middle). Quite often such side chains have lowish electron
density that does not appear at (say) 1.0 or 1.5 sigma (in the 2mFo-DFc
Typo (my fingers type faster than my brain...)
Original Message
Subject:RE: [ccp4bb] Temp Fact Variance Analysis
Date: Thu, 1 Mar 2012 14:56:06 +
From: Oganesyan, Vaheh oganesy...@medimmune.com
To: Vellieux Frederic frederic.velli...@ibs.fr
References
Hi,
The refinement program generates an mtz file with map coefficients
(including difference Fourier coefficients) so you should use that one
for model rebuilding in coot;
for the next refinement rounds, at the beginning of each round you
should provide the initial mtz file coming from data
I believe Procheck generates drawings such as those. It generates
PostScript files, and if you need to have (eg) jpg files, a PostScript
interpreter, screen capture and there you are (Gimp to select only the
areas you're interested in)
HTH,
Fred.
WENHE ZHONG wrote:
Dear memebers,
Thank
For those of you interested, the reply to Tassos' question can be found
here:
http://www.iucr.org/resources/commissions/crystallographic-computing/schools/school96/ccp4-program-system
(on-line)
as well as here, http://www.*ccp4*.ac.uk/manual.ps (a ps file).
McLaughlin, Terry and Zelinka.
There are several ways to skin a cat. If you have processed your data
with XDS, XSCALE can also do the job (you have to think of the unit cell
parameters of the merged data set though - the default may not
necessarily what you wish to have), and I am certain other data frame
processing suites
A mixture between mathematical significance and biological significance
as a part of the reply:
you should also take into account the thermal vibrations of the atoms
present in that domain, i.e. the thermal ellipsoids when you have one
of the representations of anisotropic temperature factors
Hi,
Your email mentions drop.
What about trying another technique where you do not have drops, such as the
liquid interface diffusion method (in capillaries), or the use of dialysis ?
Crystallisation
under oil (injection of the 2 components under oil) could also be tried.
Fred
Message du
D Bonsor wrote:
and allow someone else to have ago at solving the structure.
I'd be careful there if there was a motion to try to implement a policy
at SR sources (for academic research projects) to make it compulsory to
publically release all data frames after a period (1 year ? 2 years
I must say that there were some emails exchanged between me and Gerard
later, in which I pointed out that I wasn't against deposition of images
(data frames). In fact, if SR sources kept user's data there would be
one more structure from here in the PDB: HDD failure here, the data on a
mirror
Hi,
If, in your case, no possible asymmetric unit can contain A1-B2, then
you deposit A1-B1 (or I suppose A2-B2...) and indicate to the PDB (like
placing cards in the header cards) the operator to be used (and the
subunit it applies to) in order to generate the most likely biological
dimer.
Hi,
What you must deposit is what is present in the asymmetric unit of the crystal.
The HEADER cards (and the publication) can describe the most likely biological
assembly.
Why is that: there is no reason why the crystal should conform to the
biological function (and associated quaternary
Just to add to what has been said (written) before:
coiled coiled or simply helices can be very problematic for M.R.. Human
sacrifice has never given any positive result (as reported in the
literature as far as I know), but heavy atom sacrifice could be
attempted (heavy atom includes in my
Could you have an unexpected small subunit (or some other situation)
giving additional density that Phenix is building into ? In other words,
how sure are you of what is present in the crystal ? This is because I
remember the enzyme methanol dehydrogenase where there was a small
subunit which
P4(1) and P4(3) are enantiomorphic space groups. The only difference is the
helix (one way, or another). No difference in the diffraction pattern. Hence a
program (or a
crystallographer) cannot distinguish the 2 based on the diffraction pattern.
Once you start phasing, e.g. by molecular
Could be of importance to those who have to use the Lyon or Grenoble
airports (to ship in or out), check out the update from Sept. 27, 2011.
http://www.ill.eu/users/user-guide/safety/important-instructions-for-biological-samples/
Fred.
http://www.ill.eu/
Hi there,
In crystallography there are so many places where you can have problems
(and need to solve these problems) that I cannot list them all.
There is no twinning in the data - you probably mean the data does
not seem to indicate the presence of twinning but there might be
twinning;
Well in fact, it all depends on the type of detector these small angels
end up on and on the speed of this godly radiation. Only once you have
considered both these elements can you say poor little things.
My 2p worth.
Fred.
Ed Pozharski wrote:
The best X-ray related typo I ever seen was
sadaf iqbal wrote:
Hello everyone,
Do anybody know the correct procedure for calculating omit map in
CCP4, if one need to reduce the bias from the Molecular Replacement
structure. I am confused about the two options, one is fft map
calculation while the other is OMIT map calculation in Map
james09 pruza wrote:
Dear CCP4BBers,
Refmac is giving the error No reflections in resolution bin??? It
seems there is no SigFP column. I wonder how to fix the problem.
Thanks in advance.
James
If the error is indeed due to a missing SigFP column, there are 2 ways
to go about it I
Quoting you: I type ccp4 and I get no error, what happens if you type
ccp4i (followed by carriage return) ?
Yuri wrote:
I downloaded the package for RHEL5. My default shell is sh. But I can
change environments. I have progrmas that I must run in tcsh.
I tried sourcing sh and csh setups.
Hi,
It's not a bad idea to read the Phaser manual for molecular replacement;
see http://www.phaser.cimr.cam.ac.uk/index.php/Molecular_Replacement
Soon after the start, in a table on the right hand side, there is: TFZ
score 5, have I solved it ? No.
Hence with a TFZ score of 3.8 you do not
Plenty of old drives at ESRF, for that purpose. If you don't find any
other way, I could always read them there (the ESRF is in my backyard)
and burn the data to DVD for shipping (or upload to megaupload - but our
gov't is hunting down people who use such services, they think
megaupload and
Well you could have a monoclinic space group with beta = 90....0001, which
for everyone would mean 90.0 degrees. You could also have beta = exactly 90 by
pure chance. Normally the R-sym values should tell you which of the two
possibilities is the correct one.
If you obtain (an example)
The distance to your modelled water seems to be in agreement with an
ionic interaction. What are the components of all buffers in the
crystallisation components ?
Fred.
ruheng wrote:
Dear all,
Recently we are working on an archaebacteria protein which was
expressed and purified from /E.coli
Hi,
The R-factor you mention, is it an R-factor before any refinement of the
model ? Like an R-factor at the very beginning of the entire modeling
procedure, right after molecular replacement ?
If this is so: you should always compare such initial R-factors to the
R-factors for the atoms
the space group is I422 do you have any other suggestion?
Yes, how certain are you of the space group? For myself, I'm never
entirely certain of the space group until I have solved the structure...
I always keep in mind the other possibilities for space group
assignment, if need be. And
Hi,
I have a problem with the following sentence:
if I collect all spots I get good map, but it is impossible to solve
the structure by molecular replacement - if you have a good map (I
assume electron density map) then the structure is solved... for me a
good map is a map I can interpret.
Hi,
What about the ccp4 web page, from which you can follow the link to
http://www.ccp4.ac.uk/ccp4bb.php ?
HTH,
Fred.
Angela (Shaoxu) Li wrote:
Hi there,
I wish to unsubscribe to the mailing list. But I'm unsure as to how I
can do that. Your help will be greatly appreciated.
Best
Zhiyi Wei wrote:
Dear all,
I have a P2 derivative dataset with beta=89.6. I try to change the
beta to 90.4 to be consistent with the native dataset. Should I do sth
with the HKL, like applying a matrix? Thanks a million!
Best,
Zhiyi
Hi,
Personally I would use sftools (no ccp4i GUI), to
Afshan Begum wrote:
Dear All,
I have a severe prob lam to performed my ligand binding study with
corresponding protein. I have taking the native diffraction data at
1.75 A and after that i have performed soaking as well
co-crystallization experiment with my inhibitors.
Problem is that at the
Quoting you:
I wish to solve a monomeric protein in P21 where there are 2 monomers in
asymmetric unit.
How do you know that if you haven't solved the structure? Matthews coefficient
calculations?
Remember that the solvent content in protein crystal structures can go from ca.
15 % to ca. 85
Hi,
There's a whole bunch of programs that can help you out there.
The 2 methods I think of right now are DISPROT (there's a server I
believe, http://www.ist.temple.edu/disprot/ ) - Must admit I haven't
been to that one for quite a while; DISPROT provides areas of your
sequence with high
For myself, I decide on the high resolution cutoff by looking at the
Rsym vs resolution curve. The curve rises, and for all data sets I have
processed (so far) there is a break in the curve and the curve shoots
up. To near vertical. This inflexion point is where I decide to place
the high
Hi,
I don't think XDS generates an Rpim value, does it? The XDS CORRECT
strep provides the old fashioned Rsym (R-FACTOR) plus R-meas and Rmrgd-F.
The curves look all the same though
Fred.
Ed Pozharski wrote:
On Thu, 2011-03-03 at 16:02 +0100, Vellieux Frederic wrote:
For myself, I
Hi,
A Laue diffraction pattern is a diffraction pattern recorded using
polychromatic (white) radiation. Hence the beam line optics is for
focusing the radiation onto the sample (the crystal) but not to select a
single wavelength (a monochromator). Just to make it simple to understand.
Judith Reeks wrote:
Dear All,
I am currently refining a structure using the latest experimental
version of Refmac (5.6) and there seems to be a problem with my Fo-Fc
map. There is a region where I have fitted residues to the electron
density but after refinement there is still positive
Looks to me as if you have what we call ice rings, i.e. crystalline powder
diffraction. Plus what we call salt, i.e. strongly diffracting small molecule
crystal(s).
Fred.
Message du 20/02/11 14:47
De : Vandu Murugan
A : CCP4BB@JISCMAIL.AC.UK
Copie à :
Objet : [ccp4bb] Strage image
Hi Careina,
Just an example of a pir file which I just generated (using Bart Hazes
program mcfman):
P1;MALDH_
Just a title
TKVSVVGAAGTVGAAAGYNIALDIADEVVFVDIPDKEDDTVGQAADTNHGIAYDSNTRVR
QGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDYISLTTSNP
The molecular replacement program does not know about your molecule
being a single polypeptide chain. The problem is fit two bodies
therefore the program fits two bodies. The centre of mass of whatever
you wish to position is placed the standard asymmetric unit used by
the program. If it
Hi Rex,
There will be small differences in particular due to the different ways
of treating the solvent. How large of a difference are you talking
about? Normally the difference should not be very large... And if this
related to solvent effects, it will affect the low resolution
reflections
Ting-Wei Jiang wrote:
Dear experts,
Sorry for a simple question but confusing me so much!
Does it make bad effects on determining the number of identical
molecules in ASU by choosing low symmetry space group.
For example,If I choose lowest symmetry(p4) instead of higher
one(p43212).
Does
Before re-inventing the wheel...
Is there anywhere some software (freely available software, I mean) that
can add some Gaussian noise to data. The data is currently stored in a
data column in an mtz (not phase data, but amplitudes, sigma
values...) but can be exported to another format if
Fsimulated which contains the value
of column Fcalc plus 10 times a random number from a Gaussian
distribution with average = 0 and variance = 1
Cheers
-- Ian
On Fri, Feb 4, 2011 at 12:40 PM, Vellieux Frederic
frederic.velli...@ibs.fr wrote:
Before re-inventing the wheel
Hi,
I suggest that you check out the lanthanide compounds investigated by a number
of people including Richard Kahn. Papers can be found using the iucr web site
(and its search function). Commercially available.
Fred.
Message du 31/01/11 17:02
De : Jan Rashid Umar
A :
James Stroud wrote:
On Dec 20, 2010, at 1:53 PM, Jacob Keller wrote:
what is the .odp file extension?
http://tinyurl.com/mjokqs
A .odp file is an open document presentation. It is the open version
of a power point presentation.
http://en.wikipedia.org/wiki/OpenDocument
An .odp
Hi,
Last couple of times I asked myself the same question (what does it
look like?) I used ssm (or PDBeFold as seems to be called now).
http://www.ebi.ac.uk/msd-srv/ssm/
HTH,
Fred.
Liu Zhao wrote:
The structure of my protein is as shown as the purple one. Another one
,as shown as
Hi Petr,
Usually IDXREF suggests more than one Bravais lattice that is consistent
with your diffraction images;
hence it is (sometimes) worthwhile trying to INTEGRATE in all possible
Bravais lattices and this allows you to eliminate a number of
possibilities (poor profiles during integration,
Hi,
How sure are you of the space group ? What are the data processing Rsym values
(which if high may indicate mis-indexing due to an incorrect choice of detector
origin for
example) ? There are many places where things can go wrong before reaching
the molecular replacement calculation
I can't see any problem switching from Refmac to Phenix refinement. You just
provide Phenix with the current model (if you have refined using TLS there is
an additional
step, using I believe tlsanl to generate the proper PDB file as you would for
data deposition with the pdb), the initial mtz
Muhammed bashir Khan wrote:
Dear All;
I have structures of two protein one full-length while the other truncated
at the c-terminus(one from prokaryote while the other from eukaryotes).
Now I want to do the sequence alignment of these two proteins from all
species in such a way that the
Hi,
In our hands, the crystallisation droplets of glycosomal pyruvate phosphate
dikinase had a 'skin' of what I thought was denatured protein at the surface of
every crystallisation droplet. We had to learn to use the crystal microtools
(such as a microknife, or a micro-needle can't remember
Hi,
I agree with what has been mentioned about fuzzy spots. But what seems
obvious as well is that the resolution for spot picking should be
limited (to 3.5 or 4 A resolution). It is difficult to judge from an
image of a diffraction pattern, but it seems to me from this image that
the spots
I can direct you to PDB entry 1EWY, where the average isotropic
temperature factor for the major component of the complex is ca. 47 A**2
and that for the smaller component is ca. 69 A**2. Similar values than
the ones you are reporting. I am assuming some sort of disorder, or if
you prefer,
In CNS v1.2, you have the input file called model_fcalc.inp. So what I would
do is to generate these Fc's from the model, then insert them into an mtz
that contains your Fo's, and use SIGMAA to generate the Sigmaa figures of
merit. Or use another program to generate e.g. Sim weights.
HTH,
I do not know if that's really cynical: I've had the case of a referee
recommending manuscript rejection because the title of the manuscript
was not appropriate. The editor followed the advice of the referee. A
proper refereeing job would have been to suggest that the authors change
the title
Hi,
For questions relating to a specific package (if it is in rpm format, I
don't know what the Uuntu installation software uses as packages), you
can use the rpm search web site http://rpm.pbone.net/ (in addition to
http://www.rpmfind.net/ , can't search in rpmfind.net at the moment, it
Bart Hazes wrote a program (and published as well, Hazes Dijkstra perhaps)
called SSBOND I think. I cannot remember exactly what the computer program
does, but it certainly has a data base of possible disulphide bond
conformers. Hence I would myself certainly check your second didulphide to
I second that. Incorrect space group assignment usually causes this
behaviour of having R and R-free stuck at very high values. It is useful
to go back to the data processing stage and carefully consider all
Bravais lattices (and associated space groups) that the autoindexing
routine finds
I am not sure that I understand your question perfectly... You can add/remove
waters automatically during refinement using the proper options. After
refinement, then
you can also (i.e. you should also) take the output mtz file and use a graphics
program (with PDB and MTW file) for modelling
Rex Palmer wrote:
Can anyone reccomend a free download program that will calculate the
energy of a protein/ligand complex? The ligand has been modelled in.
Thanks
Rex Palmer
Birkeck College
Hi Rex,
I think any refinement program such as CNS will do this - problem is,
since these programs
Hi,
Frankly, any vendor or assembler of PC's will do. Things to make sure to
have on your PC: an NVIDIA graphics board in order to get nice graphics
(their Linux drivers are fine; I don't know their current range of
boards, here we buy middle-range boards, not the cheapest ones that are
Hi,
I did a little bit of modeling in your density (starting from a
nicotinamide ring, the positioned nicotinamide is enclosed). The middle
part looks suspiciously like a 6 membered ring. Could it be a molecule
in a half-chair conformation? There is only the blob that is
perpendicular to the
Another possibility is with sftools, set spacegroup option
Fred.
PS not in ccp4i
Graeme Winter wrote:
Hi Tim,
Is it as easy as
reindex hklin a.mtz hklout b.mtz eof
symm P43212
eof
This will simply (and correctly) reassign the symmetry operations. Is
this what you meant?
Best wishes,
ccp4i
Reflection Data Utilities
Convert to/modify/extend MTZ
Input reflection file is in XPLOR/CNS format etc
Fortran format (7X,3I5,6X,E12.4,7X,E12.4,6X,I2) Skip first 6 lines (if
# is part of the .cv file)
[I think, I have counted the space before the INDEx for example giving
me
What you could try to do is print out the pdf file, then locate a
scanner with a suitable scanning software. Several scanning software
have the possibility of generating word processing program output or
ASCII format. Since the pdf file is text only (no figures etc) then it
should be OK. You
Dear all,
Giuseppe Zaccai showed me an interesting article about science funding
(from F.T.). I thought it could be of interest to all of us since we
have to apply for funding, and succeeding in securing funds is getting
more difficult all the time.
The scan of the article can be found on:
Dear ccp4bb subscribers,
I have just learned that Proteopedia (the wikipedia-style encyclopedia
of macromolecular structures) has been voted winner in this year's
competition organized by the Scientist ( http://www.the-scientist.com/
, readers and judges choice).
So thanks to all who voted,
POST-DOCTORAL POSITION
DATE OF AVAILABILITY : starting as soon as possible, for 2 years (ANR
contract).
TITLE : purification and crystallization of ABC transporters
POSITION: the position is opened at the Institute for Structural Biology
(IBS) in Grenoble in the team of Jean-Michel Jault
Hussain Bhukyagps wrote:
Dear all,
i want to know that how can we find Rmerge from the refinements done
in CNS..??
Hi,
I think you have the terminology wrong: Rmerge (or Rsym nowadays when
most diffraction data is recorded from a single crystal) is provided by
the data frame diffraction
anna delprato wrote:
Hello All;
I've just started using XDS and have scaled three data sets from the
same crystal - unmerged. It was a SAD experiment
My question is concerning which R values to use as data processing
statistics. I don't find any Rsymm or even Redundancy values in the
LP
I would like to know the accuracy (error) of the position of the
coordinates
This is provided by the output of the refinement software.
An example (CNS-refined structure, from the pdb header, there is an
input file called xtal_pdbsubmission.inp
REMARK 3 ESTIMATED COORDINATE ERROR.
To: Vellieux Frederic frederic.velli...@ibs.fr
References: 4c57c841.2080...@ibs.fr
Dear Fred,
I think the Cruickshank Diffraction Precision Index and its specific
reformulation by David Blow are a better estimate of overall coordinate
errors.
These two papers are in Acta D.
Greetings
Hi,
You take the output mtz from the refinement program (let's assume it's
called refine_1.mtz).
Command line mode:
sftools
read refine_1.mtz col 1 2 3 4 # assuming the mtz contains H K L 2FOFCWT
PHI2FOFCWT FOFCWT PHI2FOFCWT
cal col 3FO2FCWT col 1 col 3 +
set types
F
P
F
P
R F
write
AM, Vellieux Frederic
frederic.velli...@ibs.fr wrote:
Hi,
You take the output mtz from the refinement program (let's assume it's
called refine_1.mtz).
Command line mode:
sftools
read refine_1.mtz col 1 2 3 4 # assuming the mtz contains H K L 2FOFCWT
PHI2FOFCWT FOFCWT PHI2FOFCWT
cal col 3FO2FCWT
Non-symmetric tetramers: you can check out Tete-Favier et al (1993),
Acta Cryst. D49, 246: the quaternary structure was assumed to have local
222 symmetry. It turned out this was not exactly the case: the actual
symmetry of the object (the molecule) was pseudo 2t2t2t. So in
addition to 2-fold
Hi,
To quote you: even my P222 experimental envelop does have a 4-fold
axis - this is not suprising, a particle with 222 symmetry does not
have 4-fold symmetry. There are 3 mutually perpendicular 2-fold axes
that intersect at the origin (of the particle, of the molecule) [and
for the
Vandana Kukshal wrote:
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
Hi,
I think the MAXCHN errors has been fixed in recent versions of CNS.
You must be using CNS v1.0 or v1.1.
So either you download and install a recent version (the latest is
v1.3), or you do as the error message suggests: you edit your anneal.inp
file, you locate MAXCHN= or MAXCHN = (or
News just received from the French Crystallographic Association (and
thus forwarded to ccp4bb):
The fifth Max Perutz Prize of the European Crystallographic Association
goes to to Professor Claude Lecomte from Nancy Université and CNRS, France.
Claude Lecomte is recognised for his
Hi,
Can't rotate the picture so that I can't see the distance between the
nitrogen and the green blob.
The green blob is elongated. Sometimes what happens is that you can have
2 waters (partial occupancies), in some unit cells in your crystals the
water occupies site 1, in the other unit
Hi,
If you do not know anything about peptidase (protease) classification,
I'd suggest you have a look first at the Merops peptidase data base:
http://merops.sanger.ac.uk/
Will tell you what (type of) classes there are, for example (and based
on what).
Fred.
Gowriishankar Raju wrote:
Hi there,
The way to fix or freeze an entire section of a protein molecule will
depend on the refinement program used.
For example, in CNS, I would go to the = atom selection = section in the input
file(s) and change the parameters
there. You can fix atoms, or apply harmonic restraints.
Hi,
I never carry out grouped B-factor refinement at that resolution... Also you
(probably) will want to do TLS
refinement. I think that is not possible in the current (v1.2) CNS. Implemented
in Refmac and Phenix, I don't know
if it will be implemented in the upcoming CNS v1.3.
Fred.
Hi Hui,
I think most of us can't do much with rar archive files.
This is a Windows thing I believe and my Linux system tells me
Archive type not supported...
Fred.
hui yang wrote:
Hi all,
I just collected a data set from a long-spindle-shaped crystal. The
data has been scaled to P1
Hi,
There are differences in the algorithm used by Phenix and (for example) Refmac
for the solvent treatment. These can
account for a 3 to 4 percent difference in Rfactor. I do not understand why
there is such a large discrepancy in
your case, unless you have for example a solvent model in
Received from Peter Zwart:
Message du 13/07/10 22:02
De : Peter Zwart
A : Frederic VELLIEUX , Pavel Afonine
Copie à :
Objet : Re: [ccp4bb] differences Rfactor calculations
Also, at such a high resolution you might want to do individual atomic
anisotropic temperature factor
Rsym is 0.6
I'd be seriously worried about this. An R-sym value of 0.6 in the entire
resolution range (I assume) means that your
reflection intensities do not match. This is the value of the Rsym I could
expect in the high resolution bin - in
the age of maximum likelihood refinement, not in
The rule is that the average isotropic temperature factor for your protein
atoms should not differ too wildly from the Wilson B-factor of the data set
(when you convert your anisotropic B's to isotropic B's). Otherwise there is no
such thing as an acceptable or unacceptable value, the value is
Petr Kolenko wrote:
Dear all,
I am working on crystallization of a protein purified using
intein-chitin binding domain. There is 86% identity with protein with
already known high-resolution structure, but I am not able to get any
crystals. I heard that reversed phase chromatography is not
Which own web page??? I don't have an own web page from my internet
provider, there is one at work (not everyone
at work has a such web page, in my case dedicated to PX), in order to get
something added to that web page I have to
provide the material to the person in charge of the web pages
Dear all,
A tribute to Lodovico (pictures + letters + a song) can be found on
http://www.crystalerice.org/Erice2010/Lodovico/index.htm
Fred.
Vandu Murugan wrote:
Dear all,
I have collected a 2.7 angstrom home source data with Cu-Kalpha
source for a protein with 6 cysteines, with a multiplicity of around
23. I need to know, is there any significant anamolous signal present
in the data set, since there is no good model for my
Could it be that for some reason (like the components of your solutions) you
have Mg2+ in that site? Also, Magnesium
is a common contaminant, trace amounts are usually present in one chemical or
another.
Subtle differences in the site might make it a better site for another
lighter ion (we
Dear all,
An obituary for Prof. Lodovico Riva di Sanseverino (in English, written
by Prof. Carlo Mealli) can be found on
http://www.cristallografia.org/uploaded/181.pdf
(www.cristallografia.org is the web site of the Italian Crystallographic
Association, Associazione Italiana di
To reply to the original question, can the calculated Matthews coefficient be
wrong?:
have you read the paper by Matthews? There is a distribution of solvent content
in macromolecular (protein)
crystals. It has a peak and tails on both sides. Meaning that there are
outliers in the
Dear all,
I think we all think that macromolecular structures are the best there
is... And now we have a chance to prove it to the world.
The Scientist is organizing a competition to elect the best website.
One of the competitors is the Proteopedia web site
(http://www.proteopedia.org).
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