[ccp4bb] measuring shape complementarity

[Salameh, Mohd A., Ph.D.]

Dear All,
I'm looking for a free program that I can use to measure the geometric
surface complementarity of protein-protein interfaces. I have created
inhibitor mutants that possess different binding affinities to their
cognate enzyme and it would be very helpful if I can quantify the shape
complementarity of the protein/protein interfaces. The complexes of
inhibitors and enzyme crystal structures have been solved at high
resolution (~1.4A). Sincere thanks in advance and hope to hear from you
soon.
Kind regards,
Mohd Salameh 

[ccp4bb] pH dependent conformational change

[Daniel Jin]

Dear CCP4 colleagues,

 

We have a protein that is composed of two domains
connected by a short peptide linker. We have some indirect evidence showing
that the two domains may somehow move against each other when exposed to
different pH. It is unlikely to have any obvious secondary structure change 
since
each domain behaves like a rigid body. I am wondering whether there is any 
“easy”
way, biochemically or biophysically, to monitor the conformational changes in
solution. Many thanks.

 

As far as I know most of the pH sensing stories are
linked to histidine residue. Can you point me to any references that show a
different pH sensing mechanism (other than His)? Thanks.

 

Best,

Daniel




  

Re: [ccp4bb] pH dependent conformational change

[Edward Snell]

SAXS, if the motion is not random and especially if you have 
crystallographic/NMR structure for the domains..
Edward Snell Ph.D.
Assistant Prof. Department of Structural Biology, SUNY Buffalo,
Senior Scientist, Hauptman-Woodward Medical Research Institute
700 Ellicott Street, Buffalo, NY 14203-1102
Phone: (716) 898 8631 Fax: (716) 898 8660
Skype:  eddie.snell Email: esn...@hwi.buffalo.edu
Telepathy: 42.2 GHz

Heisenberg was probably here!

From: CCP4 bulletin board [mailto:ccp...@jiscmail.ac.uk] On Behalf Of Daniel Jin
Sent: Monday, December 06, 2010 11:59 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] pH dependent conformational change


Dear CCP4 colleagues,



We have a protein that is composed of two domains connected by a short peptide 
linker. We have some indirect evidence showing that the two domains may somehow 
move against each other when exposed to different pH. It is unlikely to have 
any obvious secondary structure change since each domain behaves like a rigid 
body. I am wondering whether there is any “easy” way, biochemically or 
biophysically, to monitor the conformational changes in solution. Many thanks.



As far as I know most of the pH sensing stories are linked to histidine 
residue. Can you point me to any references that show a different pH sensing 
mechanism (other than His)? Thanks.



Best,

Daniel

Re: [ccp4bb] pH dependent conformational change

[Mischa Machius]

Daniel,

You'll probably have to monitor pH changes through size changes of your 
protein, provided the structural changes will indeed cause size changes. 

You said "easy", so that probably rules out Small-Angle X-Ray Scattering 
(SAXS), but that would be the highest-resolution method. You can try static and 
dynamic light scattering, analytical ultracentrifugation and fluorescence 
anisotropy. If you are really lucky, size exclusion chromatography might work 
too.

And then there are the "difficult" ways...

MM




On Dec 6, 2010, at 11:59 AM, Daniel Jin wrote:

> Dear CCP4 colleagues,
>  
> We have a protein that is composed of two domains connected by a short 
> peptide linker. We have some indirect evidence showing that the two domains 
> may somehow move against each other when exposed to different pH. It is 
> unlikely to have any obvious secondary structure change since each domain 
> behaves like a rigid body. I am wondering whether there is any “easy” way, 
> biochemically or biophysically, to monitor the conformational changes in 
> solution. Many thanks.
>  
> As far as I know most of the pH sensing stories are linked to histidine 
> residue. Can you point me to any references that show a different pH sensing 
> mechanism (other than His)? Thanks.
>  
> Best,
> Daniel
> 

---
Mischa Machius, PhD
Director, Center for Structural Biology
Assoc. Professor, Dept. of Pharmacology
Member, Lineberger Comprehensive Cancer Center
University of North Carolina
4079 Genetic Medicine
CB#7365
120 Mason Farm Road
Chapel Hill, NC 27599-7365, U.S.A.
tel: +1-919-843-4485
fax: +1-919-966-5640
email: mach...@unc.edu

Re: [ccp4bb] pH dependent conformational change

[Jacob Keller]

Wouldn't a HSQC of 15N-labeled protein be a relatively easy yes/no
experiment? Maybe it would not be incredibly definitive?

Jacob


On Mon, Dec 6, 2010 at 11:10 AM, Mischa Machius  wrote:

> Daniel,
>
> You'll probably have to monitor pH changes through size changes of your
> protein, provided the structural changes will indeed cause size changes.
>
> You said "easy", so that probably rules out Small-Angle X-Ray Scattering
> (SAXS), but that would be the highest-resolution method. You can try static
> and dynamic light scattering, analytical ultracentrifugation and
> fluorescence anisotropy. If you are really lucky, size exclusion
> chromatography might work too.
>
> And then there are the "difficult" ways...
>
> MM
>
>
>
>
> On Dec 6, 2010, at 11:59 AM, Daniel Jin wrote:
>
> Dear CCP4 colleagues,
>
>
>
> We have a protein that is composed of two domains connected by a short
> peptide linker. We have some indirect evidence showing that the two domains
> may somehow move against each other when exposed to different pH. It is
> unlikely to have any obvious secondary structure change since each domain
> behaves like a rigid body. I am wondering whether there is any “easy” way,
> biochemically or biophysically, to monitor the conformational changes in
> solution. Many thanks.
>
>
>
> As far as I know most of the pH sensing stories are linked to histidine
> residue. Can you point me to any references that show a different pH sensing
> mechanism (other than His)? Thanks.
>
>
>
> Best,
>
> Daniel
>
>
> ---
> Mischa Machius, PhD
> Director, Center for Structural Biology
> Assoc. Professor, Dept. of Pharmacology
> Member, Lineberger Comprehensive Cancer Center
> University of North Carolina
> 4079 Genetic Medicine
> CB#7365
> 120 Mason Farm Road
> Chapel Hill, NC 27599-7365, U.S.A.
> tel: +1-919-843-4485
> fax: +1-919-966-5640
> email: mach...@unc.edu 
>
>


-- 
***
Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
cel: 773.608.9185
email: j-kell...@northwestern.edu
***

Re: [ccp4bb] pH dependent conformational change

[Alex Shkumatov]

Hi

SAXS can be a right tool. However, how big is "short peptide linker"?

Check Nature paper by Askarieh G. and Hedhammar M. for non-His pH  
sensor.


cheers
Alex





Am 06.12.2010 um 17:59 schrieb Daniel Jin :


Dear CCP4 colleagues,

We have a protein that is composed of two domains connected by a  
short peptide linker. We have some indirect evidence showing that  
the two domains may somehow move against each other when exposed to  
different pH. It is unlikely to have any obvious secondary  
structure change since each domain behaves like a rigid body. I am  
wondering whether there is any “easy” way, biochemically or biophy 
sically, to monitor the conformational changes in solution. Many t 
hanks.


As far as I know most of the pH sensing stories are linked to  
histidine residue. Can you point me to any references that show a  
different pH sensing mechanism (other than His)? Thanks.


Best,
Daniel

Re: [ccp4bb] pH dependent conformational change

[Roopa Thapar]

If there are backbone NMR assignments available then, definately a pH titration 
using HSQCs would give site specific information.  These are easy experiments 
if someone can help you set them up.
The perturbations should map to the inter-domain interface.

If there are no assignments for the protein, spectral changes in response to pH 
would be harder to interpret.  You could try FRET by introducing two probes - 
one in each domain.

Roopa


From: CCP4 bulletin board [ccp...@jiscmail.ac.uk] On Behalf Of Jacob Keller 
[j-kell...@fsm.northwestern.edu]
Sent: Monday, December 06, 2010 12:15 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] pH dependent conformational change

Wouldn't a HSQC of 15N-labeled protein be a relatively easy yes/no experiment? 
Maybe it would not be incredibly definitive?

Jacob


On Mon, Dec 6, 2010 at 11:10 AM, Mischa Machius 
mailto:mach...@med.unc.edu>> wrote:
Daniel,

You'll probably have to monitor pH changes through size changes of your 
protein, provided the structural changes will indeed cause size changes.

You said "easy", so that probably rules out Small-Angle X-Ray Scattering 
(SAXS), but that would be the highest-resolution method. You can try static and 
dynamic light scattering, analytical ultracentrifugation and fluorescence 
anisotropy. If you are really lucky, size exclusion chromatography might work 
too.

And then there are the "difficult" ways...

MM




On Dec 6, 2010, at 11:59 AM, Daniel Jin wrote:


Dear CCP4 colleagues,



We have a protein that is composed of two domains connected by a short peptide 
linker. We have some indirect evidence showing that the two domains may somehow 
move against each other when exposed to different pH. It is unlikely to have 
any obvious secondary structure change since each domain behaves like a rigid 
body. I am wondering whether there is any “easy” way, biochemically or 
biophysically, to monitor the conformational changes in solution. Many thanks.



As far as I know most of the pH sensing stories are linked to histidine 
residue. Can you point me to any references that show a different pH sensing 
mechanism (other than His)? Thanks.



Best,

Daniel



---
Mischa Machius, PhD
Director, Center for Structural Biology
Assoc. Professor, Dept. of Pharmacology
Member, Lineberger Comprehensive Cancer Center
University of North Carolina
4079 Genetic Medicine
CB#7365
120 Mason Farm Road
Chapel Hill, NC 27599-7365, U.S.A.
tel: +1-919-843-4485
fax: +1-919-966-5640
email: mach...@unc.edu




--
***
Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
cel: 773.608.9185
email: j-kell...@northwestern.edu
***

Re: [ccp4bb] pH dependent conformational change

[Jacob Keller]

Even without assignments, wouldn't a dramatic shift be seen in the
interacting residues? Also, I suggested the method because it is
pretty easy, probably doable in a week...

Jacob

On Mon, Dec 6, 2010 at 11:24 AM, Roopa Thapar  wrote:
> If there are backbone NMR assignments available then, definately a pH 
> titration using HSQCs would give site specific information.  These are easy 
> experiments if someone can help you set them up.
> The perturbations should map to the inter-domain interface.
>
> If there are no assignments for the protein, spectral changes in response to 
> pH would be harder to interpret.  You could try FRET by introducing two 
> probes - one in each domain.
>
> Roopa
>
> 
> From: CCP4 bulletin board [ccp...@jiscmail.ac.uk] On Behalf Of Jacob Keller 
> [j-kell...@fsm.northwestern.edu]
> Sent: Monday, December 06, 2010 12:15 PM
> To: CCP4BB@JISCMAIL.AC.UK
> Subject: Re: [ccp4bb] pH dependent conformational change
>
> Wouldn't a HSQC of 15N-labeled protein be a relatively easy yes/no 
> experiment? Maybe it would not be incredibly definitive?
>
> Jacob
>
>
> On Mon, Dec 6, 2010 at 11:10 AM, Mischa Machius 
> mailto:mach...@med.unc.edu>> wrote:
> Daniel,
>
> You'll probably have to monitor pH changes through size changes of your 
> protein, provided the structural changes will indeed cause size changes.
>
> You said "easy", so that probably rules out Small-Angle X-Ray Scattering 
> (SAXS), but that would be the highest-resolution method. You can try static 
> and dynamic light scattering, analytical ultracentrifugation and fluorescence 
> anisotropy. If you are really lucky, size exclusion chromatography might work 
> too.
>
> And then there are the "difficult" ways...
>
> MM
>
>
>
>
> On Dec 6, 2010, at 11:59 AM, Daniel Jin wrote:
>
>
> Dear CCP4 colleagues,
>
>
>
> We have a protein that is composed of two domains connected by a short 
> peptide linker. We have some indirect evidence showing that the two domains 
> may somehow move against each other when exposed to different pH. It is 
> unlikely to have any obvious secondary structure change since each domain 
> behaves like a rigid body. I am wondering whether there is any “easy” way, 
> biochemically or biophysically, to monitor the conformational changes in 
> solution. Many thanks.
>
>
>
> As far as I know most of the pH sensing stories are linked to histidine 
> residue. Can you point me to any references that show a different pH sensing 
> mechanism (other than His)? Thanks.
>
>
>
> Best,
>
> Daniel
>
>
>
> ---
> Mischa Machius, PhD
> Director, Center for Structural Biology
> Assoc. Professor, Dept. of Pharmacology
> Member, Lineberger Comprehensive Cancer Center
> University of North Carolina
> 4079 Genetic Medicine
> CB#7365
> 120 Mason Farm Road
> Chapel Hill, NC 27599-7365, U.S.A.
> tel: +1-919-843-4485
> fax: +1-919-966-5640
> email: mach...@unc.edu
>
>
>
>
> --
> ***
> Jacob Pearson Keller
> Northwestern University
> Medical Scientist Training Program
> cel: 773.608.9185
> email: j-kell...@northwestern.edu
> ***
>



-- 
***
Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
cel: 773.608.9185
email: j-kell...@northwestern.edu
***

Re: [ccp4bb] pH dependent conformational change

[Roopa Thapar]

I agree that the experiment is a good one and can easily be done, but without 
assignments I think the interpretation could be ambiguous.  
 
pH dependent chemical shift perturbations could occur far removed from the 
linker (either due to a conformational change or the change in chemical 
environment around the amide nucleus) 
and without any information about which residues are shifting it may be 
difficult to conclude that these perturbations are due to a change in domain 
orientation rather than other subtle
pH dependent effects.
   
If there are no perturbations, then of course one can conclude little or no 
conformational changes occur.  The magnitude of the perturbation would depend 
on how extensive the conformational change is.

One could specifically label the protein with 15N-labeled amino acids that are 
particularly unique to the linker - this would simplify the spectrum and the 
data may be easier to interpret.

It is a good experiment to try however.


Roopa 
 

 

From: Jacob Keller [j-kell...@fsm.northwestern.edu]
Sent: Monday, December 06, 2010 12:54 PM
To: Roopa Thapar
Cc: CCP4BB@jiscmail.ac.uk
Subject: Re: [ccp4bb] pH dependent conformational change

Even without assignments, wouldn't a dramatic shift be seen in the
interacting residues? Also, I suggested the method because it is
pretty easy, probably doable in a week...

Jacob

On Mon, Dec 6, 2010 at 11:24 AM, Roopa Thapar  wrote:
> If there are backbone NMR assignments available then, definately a pH 
> titration using HSQCs would give site specific information.  These are easy 
> experiments if someone can help you set them up.
> The perturbations should map to the inter-domain interface.
>
> If there are no assignments for the protein, spectral changes in response to 
> pH would be harder to interpret.  You could try FRET by introducing two 
> probes - one in each domain.
>
> Roopa
>
> 
> From: CCP4 bulletin board [ccp...@jiscmail.ac.uk] On Behalf Of Jacob Keller 
> [j-kell...@fsm.northwestern.edu]
> Sent: Monday, December 06, 2010 12:15 PM
> To: CCP4BB@JISCMAIL.AC.UK
> Subject: Re: [ccp4bb] pH dependent conformational change
>
> Wouldn't a HSQC of 15N-labeled protein be a relatively easy yes/no 
> experiment? Maybe it would not be incredibly definitive?
>
> Jacob
>
>
> On Mon, Dec 6, 2010 at 11:10 AM, Mischa Machius 
> mailto:mach...@med.unc.edu>> wrote:
> Daniel,
>
> You'll probably have to monitor pH changes through size changes of your 
> protein, provided the structural changes will indeed cause size changes.
>
> You said "easy", so that probably rules out Small-Angle X-Ray Scattering 
> (SAXS), but that would be the highest-resolution method. You can try static 
> and dynamic light scattering, analytical ultracentrifugation and fluorescence 
> anisotropy. If you are really lucky, size exclusion chromatography might work 
> too.
>
> And then there are the "difficult" ways...
>
> MM
>
>
>
>
> On Dec 6, 2010, at 11:59 AM, Daniel Jin wrote:
>
>
> Dear CCP4 colleagues,
>
>
>
> We have a protein that is composed of two domains connected by a short 
> peptide linker. We have some indirect evidence showing that the two domains 
> may somehow move against each other when exposed to different pH. It is 
> unlikely to have any obvious secondary structure change since each domain 
> behaves like a rigid body. I am wondering whether there is any “easy” way, 
> biochemically or biophysically, to monitor the conformational changes in 
> solution. Many thanks.
>
>
>
> As far as I know most of the pH sensing stories are linked to histidine 
> residue. Can you point me to any references that show a different pH sensing 
> mechanism (other than His)? Thanks.
>
>
>
> Best,
>
> Daniel
>
>
>
> ---
> Mischa Machius, PhD
> Director, Center for Structural Biology
> Assoc. Professor, Dept. of Pharmacology
> Member, Lineberger Comprehensive Cancer Center
> University of North Carolina
> 4079 Genetic Medicine
> CB#7365
> 120 Mason Farm Road
> Chapel Hill, NC 27599-7365, U.S.A.
> tel: +1-919-843-4485
> fax: +1-919-966-5640
> email: mach...@unc.edu
>
>
>
>
> --
> ***
> Jacob Pearson Keller
> Northwestern University
> Medical Scientist Training Program
> cel: 773.608.9185
> email: j-kell...@northwestern.edu
> ***
>



--
***
Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
cel: 773.608.9185
email: j-kell...@northwestern.edu
***

[ccp4bb] helix translation

[Young-Tae Lee]

Dear colleagues,

I am analyzing a helical segment that looks a bit off from the  
traditional alpha-helix. Does anyone knows a program for calculating  
alpha helix translation per residue along the helical axis?


Thanks,
Young-Tae

Young-Tae Lee, Ph. D.
Research Associate
David Goodin lab
Dept. of Molecular Biology
The Scripps Research Institute

Re: [ccp4bb] pH dependent conformational change

[Jacob Keller]

Well, I just got word that the protein is ~100kD anyway, so I think
the HSQC is out the window anyway!

Jacob

On Mon, Dec 6, 2010 at 12:16 PM, Roopa Thapar  wrote:
>
>
> I agree that the experiment is a good one and can easily be done, but without 
> assignments I think the interpretation could be ambiguous.
>
> pH dependent chemical shift perturbations could occur far removed from the 
> linker (either due to a conformational change or the change in chemical 
> environment around the amide nucleus)
> and without any information about which residues are shifting it may be 
> difficult to conclude that these perturbations are due to a change in domain 
> orientation rather than other subtle
> pH dependent effects.
>
> If there are no perturbations, then of course one can conclude little or no 
> conformational changes occur.  The magnitude of the perturbation would depend 
> on how extensive the conformational change is.
>
> One could specifically label the protein with 15N-labeled amino acids that 
> are particularly unique to the linker - this would simplify the spectrum and 
> the data may be easier to interpret.
>
> It is a good experiment to try however.
>
>
> Roopa
>
>
>
> 
> From: Jacob Keller [j-kell...@fsm.northwestern.edu]
> Sent: Monday, December 06, 2010 12:54 PM
> To: Roopa Thapar
> Cc: CCP4BB@jiscmail.ac.uk
> Subject: Re: [ccp4bb] pH dependent conformational change
>
> Even without assignments, wouldn't a dramatic shift be seen in the
> interacting residues? Also, I suggested the method because it is
> pretty easy, probably doable in a week...
>
> Jacob
>
> On Mon, Dec 6, 2010 at 11:24 AM, Roopa Thapar  wrote:
>> If there are backbone NMR assignments available then, definately a pH 
>> titration using HSQCs would give site specific information.  These are easy 
>> experiments if someone can help you set them up.
>> The perturbations should map to the inter-domain interface.
>>
>> If there are no assignments for the protein, spectral changes in response to 
>> pH would be harder to interpret.  You could try FRET by introducing two 
>> probes - one in each domain.
>>
>> Roopa
>>
>> 
>> From: CCP4 bulletin board [ccp...@jiscmail.ac.uk] On Behalf Of Jacob Keller 
>> [j-kell...@fsm.northwestern.edu]
>> Sent: Monday, December 06, 2010 12:15 PM
>> To: CCP4BB@JISCMAIL.AC.UK
>> Subject: Re: [ccp4bb] pH dependent conformational change
>>
>> Wouldn't a HSQC of 15N-labeled protein be a relatively easy yes/no 
>> experiment? Maybe it would not be incredibly definitive?
>>
>> Jacob
>>
>>
>> On Mon, Dec 6, 2010 at 11:10 AM, Mischa Machius 
>> mailto:mach...@med.unc.edu>> wrote:
>> Daniel,
>>
>> You'll probably have to monitor pH changes through size changes of your 
>> protein, provided the structural changes will indeed cause size changes.
>>
>> You said "easy", so that probably rules out Small-Angle X-Ray Scattering 
>> (SAXS), but that would be the highest-resolution method. You can try static 
>> and dynamic light scattering, analytical ultracentrifugation and 
>> fluorescence anisotropy. If you are really lucky, size exclusion 
>> chromatography might work too.
>>
>> And then there are the "difficult" ways...
>>
>> MM
>>
>>
>>
>>
>> On Dec 6, 2010, at 11:59 AM, Daniel Jin wrote:
>>
>>
>> Dear CCP4 colleagues,
>>
>>
>>
>> We have a protein that is composed of two domains connected by a short 
>> peptide linker. We have some indirect evidence showing that the two domains 
>> may somehow move against each other when exposed to different pH. It is 
>> unlikely to have any obvious secondary structure change since each domain 
>> behaves like a rigid body. I am wondering whether there is any “easy” way, 
>> biochemically or biophysically, to monitor the conformational changes in 
>> solution. Many thanks.
>>
>>
>>
>> As far as I know most of the pH sensing stories are linked to histidine 
>> residue. Can you point me to any references that show a different pH sensing 
>> mechanism (other than His)? Thanks.
>>
>>
>>
>> Best,
>>
>> Daniel
>>
>>
>>
>> ---
>> Mischa Machius, PhD
>> Director, Center for Structural Biology
>> Assoc. Professor, Dept. of Pharmacology
>> Member, Lineberger Comprehensive Cancer Center
>> University of North Carolina
>> 4079 Genetic Medicine
>> CB#7365
>> 120 Mason Farm Road
>> Chapel Hill, NC 27599-7365, U.S.A.
>> tel: +1-919-843-4485
>> fax: +1-919-966-5640
>> email: mach...@unc.edu
>>
>>
>>
>>
>> --
>> ***
>> Jacob Pearson Keller
>> Northwestern University
>> Medical Scientist Training Program
>> cel: 773.608.9185
>> email: j-kell...@northwestern.edu
>> ***
>>
>
>
>
> --
> ***
> Jacob Pearson Keller
> Northwestern University
> Medical Scientist Training Prog

Re: [ccp4bb] helix translation

[Sergei Strelkov]

Dear Young-Tae,

The program Twister (Strelkov and Burkhard, 2002) can calculate this,
among other things. If you are interested I would gladly send you
the program.

Of course one should look into the reason for your helix having
an aberrant geometry. If it is just a slightly distorted a-helix
then you should still see the classical hydrogen bonding pattern between
the mainchain atoms.

Best wishes,
Sergei




Dear colleagues,

I am analyzing a helical segment that looks a bit off from the 
traditional alpha-helix. Does anyone knows a program for calculating 
alpha helix translation per residue along the helical axis?


Thanks,
Young-Tae

Young-Tae Lee, Ph. D.
Research Associate
David Goodin lab
Dept. of Molecular Biology
The Scripps Research Institute

Re: [ccp4bb] measuring shape complementarity

[Mike Lawrence]

Dear Mohd, CCP4 contains a program SC which does the job.

sincerely

Mike Lawrence, PhD

Associate Professor and WEHI Fellow
Division of Structural Biology
Walter and Eliza Hall Institute of Medical Research
1G Royal Parade, Parkville
Victoria 3052, AUSTRALIA

Tel. 61-3-9345-2693   
Fax 61-3-9345-2686
Email: lawre...@wehi.edu.au

On 07/12/2010, at 1:54 AM, Salameh, Mohd A., Ph.D. wrote:

> Dear All,
> 
> I’m looking for a free program that I can use to measure the geometric 
> surface complementarity of protein-protein interfaces. I have created 
> inhibitor mutants that possess different binding affinities to their cognate 
> enzyme and it would be very helpful if I can quantify the shape 
> complementarity of the protein/protein interfaces. The complexes of 
> inhibitors and enzyme crystal structures have been solved at high resolution 
> (~1.4A). Sincere thanks in advance and hope to hear from you soon.
> 
> Kind regards,
> 
> Mohd Salameh
> 
> 




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[ccp4bb] oxford cryosystems series 600 control box

[Peter Moody]

The venerable 600 series cryostream I use on our Raxis is getting too
flakey, and as they are no longer supported I cannot get it fixed. Should
anyone be thinking of sending one to the skip, I should be very pleased to
hear from you (directy).

Peter Moody
University of Leicester
Leicester UK