Re: [ccp4bb] ? steps after detwinning

[Seema Nath]

@R.Brown
I've already tried POINTLESS but due to some reasons it failed and it isyet to 
be fixed.I've used SFCHECK which shows the PST vectors.I'm alreadyusing PHASER 
with "all choices of alternative space groups".
N.B.:I've mailed you twice but each time the mail is undelivered.

[ccp4bb] Pittsburgh Diffraction Conference Oct 27-29

[Joe Ng]

This is a reminder that the 64th Annual Pittsburgh Diffraction Conference
will be in Pittsburgh Oct 27-29 at the Holiday Inn University Center.  

Registration and program information can be found at:

www.pdc2010.net




Joseph D. Ng
Associate Professor
University of Alabama in Huntsville
Huntsville, AL 35899
256-824-3715 (office), 256-824-3204 (fax)
Visit our updated website: www.uah.edu/nglab

[ccp4bb] Protein Engineering position at Zymeworks (Vancouver, Canada)

[paula lario]

Dear CCP4bb,

Structural biologists or modellers who are driven towards understanding
structure/function relationships are sought to expand our team of protein
engineers.

Zymeworks (Vancouver, Canada) is a growing biotech company, that is using
and developing computational tools for the rational design of protein
therapeutics.

http://zymeworks.com/content/careers/PDF/1243-SB_PE.pdf Note: additional
positions are also posted on our website http://zymeworks.com/careers/

Thank you, Paula Lario

Paula Lario  Ph.D.
Senior Scientist & Team Lead
Protein Engineering
Zymeworks, Inc
540-1385 West 8th Ave
Vancouver, BC
Canada V6H 3V9

[ccp4bb] Protein crystallography Postdoc Position at SLS

[Meitian Wang]

Postdoctoral Fellow
In Protein Crystallography
Your tasks
With stable light source, flexible optics, multi-axes goniometer  
(PRIGO), and advance pixel detector (PILATUS) at SLS PX beamlines,  
this postdoctoral position offers you an unique opportunity to develop  
smart diffraction data collection strategies for advanced phasing and  
challenging crystallographic projects. In order to fully exploit the  
potential of the experimental data, you will also work on the  
optimization of data processing, scaling, and structure solution  
within international collaborations. Furthermore, you are expected to  
contribute to the integration of data collection strategy, data  
processing, assessment, and structure solution procedures into the  
beamline user interface. In addition, you will conduct your own  
structural biology research in collaboration with PSI internal and  
external partners.

Your profile
You hold a PhD degree in biology, chemistry or physics, and have  
substantial experience in protein crystallography. Working knowledge  
for data processing programs, and various phasing and refinement  
software is a must. Experience in computer programming would be a  
significant advantage. If you are a good team player with fine  
communication skills and sense of responsibility, this position will  
offer a great opportunity for you to develop your research career in  
an exciting and highly multidisciplinary environment.
For further information please contact: Dr Meitian Wang, phone +41 56  
310 41 75, meitian.w...@psi.ch


Please submit your application (including CV, list of publications,  
statement of research interests and addresses of at least three  
referees) quoting the ref. code 6112-02 by e-mail to  
elke.baum...@psi.ch or to Paul Scherrer Institut, Human Resources,  
ref. code 6112-02, Elke Baumann, 5232 Villigen PSI, Switzerland.

More info: http://www.psi.ch/pa/offenestellen/Wissenschaft/2416


__
Meitian Wang
Swiss Light Source at Paul Scherrer Institut
CH-5232 Villigen PSI - http://sls.web.psi.ch
Phone: +41 56 310 4175
Fax: +41 56 310 5292

[ccp4bb] Beamline Scientist Position at SLS

[Meitian Wang]

Beamline Scientist
Protein crystallography beamline at Swiss Light Source (SLS)
Your tasks
The undulator beamline X06SA comprises two complimentary endstations,  
a high resolution and a micro-diffractometer. In order to fully  
exploit the potential of both diffractometers with advanced pixel  
detectors and multi-axes goniometry, you will conceive and implement  
novel crystallographic data acquisition tools. Furthermore, you will  
be involved in the design and development of the next generation  
protein micro-crystallography at SLS. Besides the aforementioned  
tasks, you will be in charge of beamline operation and user support.  
The position offers the opportunity to develop an independent  
scientific research programme in the field of protein crystallography  
or protein crystallographic methods development including the  
supervision of PhD students and postdocs. The infrastructure of the  
PSI Structural Biology Group will be available for you to pursue your  
own structural biology research projects.

Your profile
You hold a PhD degree in physics or (bio-)chemistry, and have several  
years of experience in synchrotron beamline instrumentation and  
protein crystallography. Knowledge of micro-diffraction techniques  
would be of advantage. If you are a good team player with fine  
communication skills and sense of responsibility, this position will  
offer a great opportunity for you to develop your research career in  
an exciting and highly multidisciplinary environment.
For further information please contact: Dr Meitian Wang, phone +41 56  
310 41 75, meitian.w...@psi.ch


Please submit your application (including CV, list of publications,  
statement of research interests and addresses of at least three  
referees) quoting the ref. code 6112-05 by e-mail to  
elke.baum...@psi.ch or to Paul Scherrer Institut, Human Resources,  
ref. code 6112-05, Elke Baumann, 5232 Villigen PSI, Switzerland.


More info: http://www.psi.ch/pa/offenestellen/Wissenschaft/2415



__
Meitian Wang
Swiss Light Source at Paul Scherrer Institut
CH-5232 Villigen PSI - http://sls.web.psi.ch
Phone: +41 56 310 4175
Fax: +41 56 310 5292

[ccp4bb] >> X-FELs and biology

[Thomas Earnest]

X-ray free electron lasers (X-FELs) offer the potential to be 
high-impact tools for research in biology, chemistry, physics, and 
materials sciences.
With FLASH and the LCLS now in operation and producing scientific 
results, and with a number of future X-FELs under construction and
development internationally, two meetings of relevance to the use of 
X-FELs in biology are taking place -


Frontiers in Biology with X-FELs  / bioXFEL20, 21 October 2010 at 
SLAChttp://www-conf.slac.stanford.edu/ssrl-lcls/2010/program.asp#BioXFEL
 (organized by Thomas Earnest, LBNL, and Garth Williams, 
LCLS/SLAC)  a joint LCLS/SSRL/ALS workshop


and

Biology with FELs   18-21 January 2011 at LBNL 
https://sites.google.com/a/lbl.gov/biology-with-fels/

 (organized by John Spence, ASU)


The goal for these workshops is to identify long and short term 
challenges of high impact in biology that X-FELs
can serve as unique, enabling resources for, and to continue to develop 
the experimental and computational
tools in this area. The input from the scientific community in shaping 
the direction for these resources over
the next ten to twenty years is critical to their success, so we 
strongly encourage your participation in these workshops.



Thomas Earnest
Garth Williams
John Spence

[ccp4bb] >> X-FELs and biology

[Thomas Earnest]

X-ray free electron lasers (X-FELs) offer the potential to be 
high-impact tools for research in biology, chemistry, physics, and 
materials sciences.
With FLASH and the LCLS now in operation and producing scientific 
results, and with a number of future X-FELs under construction and
development internationally, two meetings of relevance to the use of 
X-FELs in biology are taking place -


Frontiers in Biology with X-FELs  / bioXFEL20, 21 October 2010 at 
SLAC
http://www-conf.slac.stanford.edu/ssrl-lcls/2010/program.asp#BioXFEL
  (organized by Thomas Earnest, LBNL, and Garth Williams, 
LCLS/SLAC)  a joint LCLS/SSRL/ALS workshop


and

Biology with FELs   18-21 January 2011 at LBNL 
https://sites.google.com/a/lbl.gov/biology-with-fels/

  (organized by John Spence, ASU)


The goal for these workshops is to identify long and short term 
challenges of high impact in biology that X-FELs
can serve as unique, enabling resources for, and to continue to develop 
the experimental and computational
tools in this area. The input from the scientific community in shaping 
the direction for these resources over
the next ten to twenty years is critical to their success, so we 
strongly encourage your participation in these workshops.



Thomas Earnest
Garth Williams
John Spence

Re: [ccp4bb] Lousy diffraction at home but fantastic at the synchrotron?

[Phil Jeffrey]

Often this reflect crystal size - a small crystal in a big beam (or one 
with a long path in air) on a home source would see the small 
diffraction signal drop below the noise level quite quickly - often at 
the low resolution intensity dip that sits very approximately around 6 
Angstrom.  On a synchrotron source with a tight low-divergence beam that 
matches more closely the crystal dimensions that same crystal will 
appear to do rather better.


Also one is more likely to expose the crystal longer (in terms of total 
photon numbers) at a synchrotron, which itself begets better signal/noise.


Alternatively: everyone tries harder before synchrotron trips

Phil Jeffrey
Princeton

On 9/28/10 1:27 PM, Francis E Reyes wrote:

Hi all

I'm interested in the scenario where crystals were screened at home and
gave lousy (say < 8-10A) but when illuminated with synchrotron radiation
gave reasonable diffraction ( > 3A) ? Why the discrepancy?

Thanks

F

Re: [ccp4bb] ? steps after detwinning

[Seema Nath]

@R.Brown
I regret to say that I can't tell what the actual translation is but
regarding no. of monomers/asu,I got three non-overlapping monomers.My
problems are -
1.actual space-group is not clear yet.
2.no. of monomers/asu ?
3.how to proceed with the technique where data having pseudosymmetry &
twinning are firstly solved in lower symmetry space-group until the
R-factor & R-free come to stand still and then tranference to a higher
symmetry space-group.Is the solution in lower symmetry sg used in higher
symmetry sg or the raw data is individually processed in both lower &
higher sg?
I've mentioned the detailed problem in the ccp4bb on 27th september'10

Re: [ccp4bb] Lousy diffraction at home but fantastic at the synchrotron?

[Ethan Merritt]

On Tuesday 28 September 2010 10:27:17 am Francis E Reyes wrote:
> Hi all
> 
> I'm interested in the scenario where crystals were screened at home  
> and gave lousy (say < 8-10A) but when illuminated with synchrotron  
> radiation gave reasonable diffraction ( > 3A) ? Why the discrepancy?

Such a happy outcome is very rare.

I normally expect the high intensity at a beamline to push the line
separating "weak but visible" and "too weak to see" towards higher
resolution usable data.  But that isn't a change in the diffracting
properties of the crystal, just a change in achievable signal-to-noise.

Two possibilities come to mind.

A) Unintentional annealing during transport/or and as a consequence of
   crystal handling after shipment.  We've certainly seen this, but
   usually the result is bad ice rings rather than better diffraction. 

B) Home screening used a relatively large beam that saw the entirely 
   of a highly imperfect crystal.  The synchrotron beam used a much
   smaller aperture that happened to illuminate only a sweet spot.
   This is one argument advanced for the use of micro-focus beams.

B') An extreme case of B.  Multiple crystals in the loop.
   Home screening caught a bad one; beamline screening caught a good one.

-- 
Ethan A Merritt
Biomolecular Structure Center,  K-428 Health Sciences Bldg
University of Washington, Seattle 98195-7742

Re: [ccp4bb] Lousy diffraction at home but fantastic at the synchrotron?

[Van Den Berg, Bert]

I find this interesting as well, mainly because I have never seen this myself 
and I have looked at plenty of badly diffracting crystals. In my hands, 
synchrotron data at most end up being ~1.5 angstrom better in terms of 
resolution than the same crystals on our home source. I'm wondering if this 
phenomenon is real, or whether it is just a matter of people screening 
more/better crystals at the synchrotron compared to at home? Or a lousy home 
source?

Bert


On 9/28/10 1:27 PM, "Francis E Reyes"  wrote:

Hi all

I'm interested in the scenario where crystals were screened at home
and gave lousy (say < 8-10A) but when illuminated with synchrotron
radiation gave reasonable diffraction ( > 3A) ? Why the discrepancy?

Thanks

F

-
Francis E. Reyes M.Sc.
215 UCB
University of Colorado at Boulder

gpg --keyserver pgp.mit.edu --recv-keys 67BA8D5D

8AE2 F2F4 90F7 9640 28BC  686F 78FD 6669 67BA 8D5D

[ccp4bb] Lousy diffraction at home but fantastic at the synchrotron?

[Francis E Reyes]

Hi all

I'm interested in the scenario where crystals were screened at home  
and gave lousy (say < 8-10A) but when illuminated with synchrotron  
radiation gave reasonable diffraction ( > 3A) ? Why the discrepancy?


Thanks

F

-
Francis E. Reyes M.Sc.
215 UCB
University of Colorado at Boulder

gpg --keyserver pgp.mit.edu --recv-keys 67BA8D5D

8AE2 F2F4 90F7 9640 28BC  686F 78FD 6669 67BA 8D5D

Re: [ccp4bb] .cv to .mtz conversion

[Ian Tickle]

Hi,

There are 2 basic ways of approaching this problem: the good and the
bad (I won't even mention the ugly!).  The bad ways all involve
counting columns and working out Fortran formats.  This is because it
cannot be safely assumed that the file has been written with fixed
length records, which is the basic assumption you're making when you
specify a Fortran format.  If the file was written using Fortran 'G'
(general) format then some numbers might appear as (for example)
'123.456' whereas others might come out as (say) 1.23456E+10.  There's
no way a fixed format read can handle both of these.  Added to that,
working out a Fortran format is surely very error-prone, as evidenced
by the number of questions posted to the BB from people who have
attempted it!  If you get it wrong and you're lucky the program will
crash and you'll know you have to try one of the 'good' ways.  If
you're unlucky the program will run to completion and produce a
success status, but in reality some reflections will have been
assigned the wrong values, and you'll probably never know that it
didn't actually work.

The only safe way is to treat the file as free format: there are a
number of 'good' ways, some of which have been mentioned (e.g.
convert2mtz, phenix.refine).  Might I also suggest that you Read The
Fine Manual, specifically of the f2mtz program, which is the CCP4
utility which does this conversion.  This advises converting the file
first to free format using a little perl script (I know there are
other and no doubt equally reliable scripts around), which completely
circumvents column-counting and the fixed Fortran format trap.

If convert2mtz or any of the 'approved' ways didn't work, I would
encourage you to report it: that way if the program is at fault and it
gets fixed then everyone benefits; if you did something wrong then at
least you'll end up a little wiser.

Cheers

-- Ian

On Tue, Sep 28, 2010 at 3:41 PM, Jeremiah Farelli  wrote:
> We recently had this problem in our lab.
>
> No matter what we tried, we could not get convert2mtz (or any other program) 
> to work properly.  We were probably doing something wrong with the 
> fortran?
>
> Depending on how far along you are, you can try using phenix.refine.  Just 
> input your model and the .cv file and phenix will export a new .cv file with 
> Free-R flags intact.
>
> If you aren't to the model building stage yet, this won't work however.

Re: [ccp4bb] .cv to .mtz conversion

[Tim Gruene]

You can use the command
sed -e "s/INDEx\(.*\) FOBS= \(.*\) SIGMA= \(.*\) TEST=\(.*\)/\1 \2 \3 \4/g" 
file.cv > file.hkl

in order to get rid of all the words and convert the file into a simple
hkl-file. After removing the header you can use f2mtz to convert it to an
mtz-file.
Make sure that you DO NOT use a FORMAT line in f2mtz since it will then use free
format to read in the hkl-file, which will separate the entries by white spaces.

Tim


On Tue, Sep 28, 2010 at 03:41:29PM +0100, Jeremiah Farelli wrote:
> We recently had this problem in our lab.  
> 
> No matter what we tried, we could not get convert2mtz (or any other program) 
> to work properly.  We were probably doing something wrong with the 
> fortran?
> 
> Depending on how far along you are, you can try using phenix.refine.  Just 
> input your model and the .cv file and phenix will export a new .cv file with 
> Free-R flags intact.  
> 
> If you aren't to the model building stage yet, this won't work however. 
-- 
--
Tim Gruene
Institut fuer anorganische Chemie
Tammannstr. 4
D-37077 Goettingen

GPG Key ID = A46BEE1A



signature.asc
Description: Digital signature

Re: [ccp4bb] .cv to .mtz conversion

[Stuart Endo-Streeter]

Look up fortran formatting via google, it's all there.  You have to
enter the fortan format to match the format of the cv file.

Conceptually something like:
3F3.0, 14X, F10.3, 12X, F10.3
which means

Three fields with values to import, each of three columns with no
decimal points
skip 14 columns
One field, 10 columns, three are after the decimal point
skip 12 columns
One field, 10 columns, three are after the decimal point



On Tue, 2010-09-28 at 15:41 +0100, Jeremiah Farelli wrote:
> We recently had this problem in our lab.  
> 
> No matter what we tried, we could not get convert2mtz (or any other program) 
> to work properly.  We were probably doing something wrong with the 
> fortran?
> 
> Depending on how far along you are, you can try using phenix.refine.  Just 
> input your model and the .cv file and phenix will export a new .cv file with 
> Free-R flags intact.  
> 
> If you aren't to the model building stage yet, this won't work however. 
-- 








__
Stuart Endo-Streeter, Ph.D
Dept. Computer Science
3245 French Family Science Center
Duke University
Durham, NC 27710
919-660-4018
stuart.endostree...@duke.edu

Re: [ccp4bb] .cv to .mtz conversion

[Pavel Afonine]

We recently had this problem in our lab.

No matter what we tried, we could not get convert2mtz (or any other program) to 
work properly.  We were probably doing something wrong with the fortran?

Depending on how far along you are, you can try using phenix.refine.  Just 
input your model and the .cv file and phenix will export a new .cv file with 
Free-R flags intact.


One more options:

"Reflection file editor" from PHENIX GUI can convert most of any known 
reflection data formats into MTZ. You will also have options to rename 
labels, create r-free-flags, combine multiple input files (in different 
formats) into one MTZ, and more.


Pavel.

Re: [ccp4bb] .cv to .mtz conversion

[Jeremiah Farelli]

We recently had this problem in our lab.  

No matter what we tried, we could not get convert2mtz (or any other program) to 
work properly.  We were probably doing something wrong with the fortran?

Depending on how far along you are, you can try using phenix.refine.  Just 
input your model and the .cv file and phenix will export a new .cv file with 
Free-R flags intact.  

If you aren't to the model building stage yet, this won't work however. 

Re: [ccp4bb] .cv to .mtz conversion

[Kevin Cowtan]

You could try:

convert2mtz -hklin my.cv -mtzout my.mtz -cell 
30.0,40.0,50.0,90.0,90.0,90.0 -spacegroup 'P 21 21 21'


Marni Williams wrote:


Hey
 
I have a problem with converting a CNS created file in .cv format to 
.mtz for use in CCP4. I suspect it is because the Fortran model and the 
column labels are incorrect but I have no idea how to fix this. Here are 
the first few lines of the .cv  file:
 
###

NREFlection=   98435
  ANOMalous=FALSe
  DECLare NAME=FOBS  DOMAin=RECIprocal   TYPE=REAL END
  DECLare NAME=SIGMA DOMAin=RECIprocal   TYPE=REAL END
  DECLare NAME=TEST  DOMAin=RECIprocal   TYPE=INTE END
 INDEx002 FOBS=  0.2276E+02 SIGMA=  0.1094E+02 TEST= 0
 INDEx003 FOBS=  0.8401E+03 SIGMA=  0.9090E+01 TEST= 0
 INDEx004 FOBS=  0.1032E+04 SIGMA=  0.1418E+02 TEST= 0
##

any advice would be greatly appreciated.
 
Regards,

Marni Williams


--
Molecular Parasitology Laboratory
Department of Biochemistry
School of Biological Sciences
Faculty of Natural and Agricultural Sciences
University of Pretoria
Pretoria
South Africa
0002

Tel: +27 12 420 2990
Fax: +27 12 362 5302
Email: ma...@tuks.co.za 




--
EMAIL DISCLAIMER http://www.york.ac.uk/docs/disclaimer/email.htm

Re: [ccp4bb] .cv to .mtz conversion

[Vellieux Frederic]

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 7X; basically it's a question of counting the characters in the INDEx 
records]


HTH,

Fred.

Marni Williams wrote:


Hey
 
I have a problem with converting a CNS created file in .cv format to 
.mtz for use in CCP4. I suspect it is because the Fortran model and 
the column labels are incorrect but I have no idea how to fix this. 
Here are the first few lines of the .cv  file:
 
###

NREFlection=   98435
  ANOMalous=FALSe
  DECLare NAME=FOBS  DOMAin=RECIprocal   TYPE=REAL END
  DECLare NAME=SIGMA DOMAin=RECIprocal   TYPE=REAL END
  DECLare NAME=TEST  DOMAin=RECIprocal   TYPE=INTE END
 INDEx002 FOBS=  0.2276E+02 SIGMA=  0.1094E+02 TEST= 0
 INDEx003 FOBS=  0.8401E+03 SIGMA=  0.9090E+01 TEST= 0
 INDEx004 FOBS=  0.1032E+04 SIGMA=  0.1418E+02 TEST= 0
##

any advice would be greatly appreciated.
 
Regards,

Marni Williams


--
Molecular Parasitology Laboratory
Department of Biochemistry
School of Biological Sciences
Faculty of Natural and Agricultural Sciences
University of Pretoria
Pretoria
South Africa
0002

Tel: +27 12 420 2990
Fax: +27 12 362 5302
Email: ma...@tuks.co.za 

[ccp4bb] .cv to .mtz conversion

[Marni Williams]

Hey

I have a problem with converting a CNS created file in .cv format to .mtz
for use in CCP4. I suspect it is because the Fortran model and the column
labels are incorrect but I have no idea how to fix this. Here are the first
few lines of the .cv  file:

###
NREFlection=   98435
  ANOMalous=FALSe
  DECLare NAME=FOBS  DOMAin=RECIprocal   TYPE=REAL END
  DECLare NAME=SIGMA DOMAin=RECIprocal   TYPE=REAL END
  DECLare NAME=TEST  DOMAin=RECIprocal   TYPE=INTE END
 INDEx002 FOBS=  0.2276E+02 SIGMA=  0.1094E+02 TEST= 0
 INDEx003 FOBS=  0.8401E+03 SIGMA=  0.9090E+01 TEST= 0
 INDEx004 FOBS=  0.1032E+04 SIGMA=  0.1418E+02 TEST= 0
##

any advice would be greatly appreciated.

Regards,
Marni Williams


-- 
Molecular Parasitology Laboratory
Department of Biochemistry
School of Biological Sciences
Faculty of Natural and Agricultural Sciences
University of Pretoria
Pretoria
South Africa
0002

Tel: +27 12 420 2990
Fax: +27 12 362 5302
Email: ma...@tuks.co.za

[ccp4bb] Post-doc vacancies in London

[Dale Wigley]

The Institute of Cancer Research
(University of London)

Section of Structural Biology
Chelsea, London

Post-doctoral Training Fellows

Structural Biology of proteins involved in DNA repair

Postdoctoral positions are available to join a team in the laboratory of
Prof. Dale Wigley, FRS, who has recently relocated to the Institute of
Cancer Research. The project will be to study the structure and mechanism of
proteins involved in DNA double-strand break repair, a key aspect in the
prevention of cancers. Studies will include the bacterial RecBCD and AddAB
complexes as well as the human DNA double-strand break repair complexes,
several of which are already expressed and purified. The postholder/s will
will join a team of international scientists with a diverse range of
structural and biochemical expertise working closely together and will be
responsible for expression, purification, crystallization and structural
analysis of proteins and protein complexes either by crystallography or
electron microscopy.

The Institute of Cancer Research (a College of the University of London) is
a world-class cancer research organisation. The Section of Structural
Biology at ICR is exceptionally well equipped for all aspects of modern
structural biology, with state-of-the-art laboratories for molecular
biology, recombinant expression in bacterial and eukaryotic systems,
biochemistry, X-ray crystallography and electron microscopy. Excellent
synchrotron access (~ 2 days per month) is available through rolling beam
allocation programmes at Diamond and ESRF.

Applicants should hold a PhD in a biological, chemical or physical science,
have experience of macromolecular crystallography and recombinant protein
expression, and evidence of a good publication record. Experience in
determining structures by MIR or MAD, or of single particle electron
microscopy would be an advantage.

The starting salary will be in the range £26,996 to £32,024 p.a. inclusive
(based on previous post-doctoral experience) and posts will be offered on 3
year fixed term contracts initially.

For further particulars and details of how to apply, please visit our
website at www.icr.ac.uk  . Alternatively you may call
our 24 hour recruitment line on 020 7153 5475 quoting job reference number
C370.

Closing date: 31st October 2010


This communication is from Cancer Research UK. Our website is at 
www.cancerresearchuk.org. We are a registered charity in England and Wales 
(1089464) and in Scotland (SC041666) and a company limited by guarantee 
registered in England and Wales under number 4325234. Our registered address is 
61 Lincoln's Inn Fields, London WC2A 3PX. Our central telephone number is 020 
7242 0200.

>From 1 October 2010 our registered address will be Angel Building, 407 St John 
>Street, London, EC1V 4AD.  
 
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