[ccp4bb] Faculty equivalent cryoEM position

[Hasan, Syed Saif]

**

Faculty-Equivalent, Cryo-Electron Microscopy (Cryo-EM)



Position Summary:

As part of its program focused on advancing new measurement technologies and 
standards for biomolecular structure and function, the National Institute for 
Standards and Technology (NIST) Biomolecular Structure & Function Group seeks a 
‘faculty-equivalent’ principle investigator to establish a research program 
focused on applications of cryo-electron microscopy (cryo-EM) in structural 
biology.  We are particularly interested in candidates with a focus on 
developing cryo-EM experimental techniques and data analysis tools, and who 
would leverage other structure methods [e.g. nuclear magnetic resonance (NMR), 
macromolecular crystallography and/or small angle scattering], to advance the 
current state-of-the-art in structure-function analysis of biological systems 
of biopharmaceutical interest.



The successful candidate should have a PhD or equivalent, a strong research 
portfolio and publication record that demonstrates evidence of cryo-EM 
expertise complementary to current group research strengths in NMR, 
crystallography and small angle scattering.  He/she is expected to become a 
recognized leader in the field of cryo-EM and contribute to collaborative 
projects both within the group and with external partners.  US Citizenship is 
required.



The Biomolecular Structure & Function Group is located at the Institute for 
Bioscience and Biotechnology Research (IBBR), a joint 
federal-state research partnership between NIST and the University of Maryland. 
 IBBR operates state-of-the-art research facilities and is located in the heart 
of the biotechnology corridor in Rockville, Maryland. The Biomolecular 
Structure & Function Group is affiliated with the NIST Center for Neutron 
Research (NCNR) and the NIST 
Biomanufacturing
 program. Our cryo-EM facility located at IBBR includes a newly installed 200 
kV Talos-Arctica equipped with a Falcon III direct electron detector. A K3 
direct electron detector and a Volta phase plate will be acquired soon in 
addition to a 200 kV Glacios microscope. State-of-the-art computational 
resources are available through the IBBR High Performance Computing Cluster.



Salary: Commensurate with qualifications.



Applications: Applicants should send cover letter, curriculum vitae, research 
statement, and contact information of three references to the attention of John 
P. Marino, Leader, Biomolecular Structure & Function Group: 
john.mar...@nist.gov.

**

S. Saif Hasan, PhD


Assistant Professor

Department of Biochemistry and Molecular Biology

University of Maryland School of Medicine

108 N. Greene St., Baltimore, MD 21201


Group Leader

Center for Biomolecular Therapeutics (CBT)

Institute for Bioscience and Biotechnology Research (IBBR)

9600 Gudelsky Drive, Rockville, MD 20850

Phone: 240-314-6396

https://www.ibbr.umd.edu/profiles/s-saif-hasan



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Re: [ccp4bb] Re-using 96-well crystallization plates

[Javier Gonzalez]

Hello Nemanja,
I used to wash and reuse glass plates for neutron crystallography. Of
course glass is sturdier than polystyrene, but I can't think of any protein
stain that would resist a treatment with detergent, then a strong base (say
0.1M NaOH) and finally a strong acid (say 0.1M HCl)...
Regarding the drop shape problem that Janet mentioned, we applied Sigmacote
to the dry clean plates, a siliconizing agent sold by Sigma Aldrich, which
turns the surface non-adherent and chemically inert. From the website:
*Sigmacote® is a solution of a chlorinated organopolysiloxane in heptane
that readily forms a covalent, microscopically thin film on glass. The film
repels water, retards the clotting of blood or plasma, and prevents surface
adsorption of many basic proteins.*
However, I don't know whether polystyrene would resist the heptane solvent,
but the applied coat is very thin and should evaporate quickly if let dry
in a hood with the fan on.
I hope this helps and please let me know if it works!!
Best wishes,
Javier


On Wed, Apr 10, 2019 at 8:11 PM Newman, Janet (Manufacturing, Parkville)
 wrote:

> Hi Nemanja,
>
>
>
> I have tried doing this, and it has never really worked for me, even with
> careful rinsing with MilliQ water after washing, I could never get
> well-shaped drops on a recycled plate. They are also a real pain to wash
> out, and it’s hard to get the last traces of protein out of the subwells
> without scratching the subwells. (I was also doing this with the
> polystyrene SD-2 plates from SwissSci)
>
>
>
> Janet
>
>
>
> *From:* CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] *On Behalf Of 
> *Nemanja
> Vuksanovic
> *Sent:* Thursday, 11 April 2019 4:42 AM
> *To:* CCP4BB@JISCMAIL.AC.UK
> *Subject:* [ccp4bb] Re-using 96-well crystallization plates
>
>
>
> Dear All,
>
>
>
> I'd like to ask if anyone has experience cleaning old 96 well
> crystallization plates? I have a large number of old plates (Swissci) with
> mostly INDEX and PEG Ion screens and I thought of re-using them instead of
> throwing them away, but I'm not sure if this would be viable.
>
>
>
> Best regards,
>
>
>
> Nemanja Vuksanovic
>
>
> --
>
> Graduate Student
>
> Department of Chemistry and Biochemistry
>
> University of Wisconsin-Milwaukee
>
>
>
>
>
>
> --
>
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1
>
> --
>
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1
>


-- 
Dr. Javier M. González
Instituto de Bionanotecnología del NOA (INBIONATEC-CONICET)
Universidad Nacional de Santiago del Estero (UNSE)
RN9, Km 1125. Villa El Zanjón. (G4206XCP)
Santiago del Estero. Argentina
Tel: +54-(0385)-4238352
Email  LinkedIn




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Re: [ccp4bb] Re-using 96-well crystallization plates

[Newman, Janet (Manufacturing, Parkville)]

Hi Nemanja,

I have tried doing this, and it has never really worked for me, even with 
careful rinsing with MilliQ water after washing, I could never get well-shaped 
drops on a recycled plate. They are also a real pain to wash out, and it’s hard 
to get the last traces of protein out of the subwells without scratching the 
subwells. (I was also doing this with the polystyrene SD-2 plates from SwissSci)

Janet

From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Nemanja 
Vuksanovic
Sent: Thursday, 11 April 2019 4:42 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Re-using 96-well crystallization plates

Dear All,

I'd like to ask if anyone has experience cleaning old 96 well crystallization 
plates? I have a large number of old plates (Swissci) with mostly INDEX and PEG 
Ion screens and I thought of re-using them instead of throwing them away, but 
I'm not sure if this would be viable.

Best regards,

Nemanja Vuksanovic

--
Graduate Student
Department of Chemistry and Biochemistry
University of Wisconsin-Milwaukee





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[ccp4bb] Call for Stanford-SLAC Cryo-EM Center (S2C2) Applications: Deadline June 1, 2019

[Dunn, Lisa B.]

Dear All,

The second deadline for submitting proposals to the Stanford-SLAC Cryo-EM 
Center (S2C2) is coming up soon.Please apply at  
https://userportal.slac.stanford.edu/  by June 1.

The missions of the Stanford-SLAC Cryo-EM Center (S2C2) are:

  1.  to provide access to state-of-the-art cryo-EM instruments for data 
collection towards atomic resolution structure determination of biochemically 
purified single particles
  2.  to enable scientists across the nation to become independent cryo-EM 
investigators
More information about the S2C2 program and the project application process is 
available at:  https://cryoem.slac.stanford.edu/s2c2/.

Best regards,

Lisa Dunn
Stanford-SLAC Cryo-EM Center (S2C2)
SLAC National Accelerator Laboratory
2575 Sand Hill Rd.
Menlo Park, CA 94025
l...@slac.stanford.edu




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Re: [ccp4bb] A Max Perutz question

[Zachary A. Wood]

Thank you to everyone who responded.
I have a request in at both Nature (thanks Jonathan Davies and Daniel Bonsor 
for the article link) and also to the LMB (thanks to Harry Powell for helping 
me find the right person to talk to). A special thank you to my dear friend 
Savvas Savvides, who pointed me to Georgina Ferry’s biography of Max Perutx 
(Max Perutz and the secret of life). After a quick trip to the library, I now 
have a much better photo.

Best regards,

Z


***
Zachary A. Wood, Ph.D.
Associate Professor and Graduate Coordinator
Department of Biochemistry & Molecular Biology
University of Georgia
Life Sciences Building, Rm A426B
120 Green Street
Athens, GA  30602-7229
Office: 706-583-0304
Lab:706-583-0303
FAX: 706-542-1738
***

On Apr 10, 2019, at 11:38 AM, Savvas Savvides 
mailto:savvas.savvi...@ugent.be>> wrote:

Hey Zac
A good scan of page 228 in Georgina Ferry’s biography of Max Perutx (Max Perutz 
and the secret of life) will do the trick. It is a 18x13 cm photo. I have it in 
front of me!

best
Savvas

On 10 Apr 2019, at 16:29, Zachary A. Wood mailto:z...@uga.edu>> 
wrote:

Hello Fellow Structural Enthusiasts,

My apologies for the slightly off-topic question. I am trying to track down a 
higher resolution image of the jpg that I have attached. I use this photo of 
Max Perutz when I am teaching about protein folding, and have always wanted a 
better quality one. I believe it is credited to Nature, and I am trying to find 
out what issue, but I am hoping that one of you may have more information or 
perhaps even a better photo. Thanks for any help, and for those of you who may 
never have seen this photo before, I hope you enjoy it. I like to imagine that 
Perutz is considering the challenges associated with folding that chain after 
he determined the crystal structure. If you have never read the discussion in 
his famous Nature paper, I will leave you with a relevant quote of him 
referring to the structural similarity between horse hemoglobin and sperm whale 
myoglobin, in which he predicts the thermodynamic hypothesis (Anfinsen’s dogma):

“How does this arise? It is scarcely conceivable that a three-dimensional 
template forces the chain to take up this fold. More probably, the chain, once 
synthesized and provided with a haem group around which it can coil, takes up 
this configuration spontaneously, as the only one which satisfies the 
stereochemical requirements of its amino acid sequence.”

Thank you for any help you may be able to offer!

 Best regards,

Z

***
Zachary A. Wood, Ph.D.
Associate Professor and Graduate Coordinator
Department of Biochemistry & Molecular Biology
University of Georgia
Life Sciences Building, Rm A426B
120 Green Street
Athens, GA  30602-7229
Office: 706-583-0304
Lab:706-583-0303
FAX: 706-542-1738
***




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Re: [ccp4bb] Coot issue with add residue

[Eleanor Dodson]

Yes, Christian - that has happened to me. I found it by using the
Validation Density fit., and noticing that a residue number which was not
meant to exist had a Density fit bar.   As you say there was a stray atom
with that ID - totally incorrect - in the coordinate file..

Eleanor

On Wed, 10 Apr 2019 at 19:41, Christian Roth 
wrote:

> Well I think I recall one instance where it worked for me the way you
> describe. I think there was either a stray residue atom somewhere or a
> numbering not quite right. Could it be that this happens for you after
> autobuilding?
>
> Cheers
>
> On Wed, Apr 10, 2019 at 7:11 PM Hillen, Hauke 
> wrote:
>
>> Dear all,
>>
>> Thank you for your many suggestions!
>> Indeed, I was not able to fix the issue to my satisfaction. As Paul
>> suspected, set_add_terminal_residue_do_post_refine was already set to 0.
>> The triple-refine also did not improve anything. I also checked for the TER
>> records, which I also suspected first, but there are none in my PDB file.
>>
>> The workaround solution was to delete a larger number of residues and
>> eventually start adding from the opposite end of the chain I was adding
>> previously. For some reason, this worked in multiple instances. However, it
>> was a trial-and-error of how many residues I had to first remove and then
>> re-add to make it work.
>>
>> I am still puzzled by this - please let me know if anybody ever gets to
>> the root of this.
>>
>> Kind regards,
>> Hauke
>> 
>>
>> To unsubscribe from the CCP4BB list, click the following link:
>> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1
>>
>
> --
>
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1
>



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[ccp4bb] Re-using 96-well crystallization plates

[Nemanja Vuksanovic]

Dear All,

I'd like to ask if anyone has experience cleaning old 96 well crystallization 
plates? I have a large number of old plates (Swissci) with mostly INDEX and PEG 
Ion screens and I thought of re-using them instead of throwing them away, but 
I'm not sure if this would be viable.

Best regards,

Nemanja Vuksanovic

--
Graduate Student
Department of Chemistry and Biochemistry
University of Wisconsin-Milwaukee






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Re: [ccp4bb] Coot issue with add residue

[Christian Roth]

Well I think I recall one instance where it worked for me the way you
describe. I think there was either a stray residue atom somewhere or a
numbering not quite right. Could it be that this happens for you after
autobuilding?

Cheers

On Wed, Apr 10, 2019 at 7:11 PM Hillen, Hauke 
wrote:

> Dear all,
>
> Thank you for your many suggestions!
> Indeed, I was not able to fix the issue to my satisfaction. As Paul
> suspected, set_add_terminal_residue_do_post_refine was already set to 0.
> The triple-refine also did not improve anything. I also checked for the TER
> records, which I also suspected first, but there are none in my PDB file.
>
> The workaround solution was to delete a larger number of residues and
> eventually start adding from the opposite end of the chain I was adding
> previously. For some reason, this worked in multiple instances. However, it
> was a trial-and-error of how many residues I had to first remove and then
> re-add to make it work.
>
> I am still puzzled by this - please let me know if anybody ever gets to
> the root of this.
>
> Kind regards,
> Hauke
> 
>
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1
>



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Re: [ccp4bb] Coot issue with add residue

[Hillen, Hauke]

Dear all,

Thank you for your many suggestions!
Indeed, I was not able to fix the issue to my satisfaction. As Paul suspected, 
set_add_terminal_residue_do_post_refine was already set to 0. The triple-refine 
also did not improve anything. I also checked for the TER records, which I also 
suspected first, but there are none in my PDB file.

The workaround solution was to delete a larger number of residues and 
eventually start adding from the opposite end of the chain I was adding 
previously. For some reason, this worked in multiple instances. However, it was 
a trial-and-error of how many residues I had to first remove and then re-add to 
make it work.

I am still puzzled by this - please let me know if anybody ever gets to the 
root of this.

Kind regards,
Hauke


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[ccp4bb] ARP/wARP awk: Command not found.

[wtempel]

Hi,
auto_tracing.sh “ARP/wARP 8.0 patch 1”, after a few cycles, prints
awk: Command not found., and exits a little later with:

 Data line --  RESOLUTION 20 2.2
 Data line --  REMOVE ATOMS 8 CUTSIGMA 1.0 FORCE NEGATIVE MERGE 0.7
 Data line --  FIND   ATOMS  CHAIN Z CUTSIGMA 3.2 RESN DUM

 This Data Card is not understood:

 FIND   ATOMS  CHAIN Z CUTSIGMA 3.2 RESN DUM
 Looking for keyword ATOM followed by  1 field(s)
 Cannot accept field shown by arrows:

 FIND   ATOMS ==>CHAIN<== Z CUTSIGMA 3.2 RESN DUM

 Expected format:

 FIND ATOMS number CHAIN string CUTSIGMA number/AUTO RESNAM WAT/DUM

I do not know if the last error message is related to awk. In any case, awk
is available in /usr/bin/awk.
Did anyone else experience this issue? If so, is there a workaround?
Thanks.
Wolfram Tempel



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Re: [ccp4bb] A Max Perutz question

[Mitchell D. Miller]

You can also do a reverse image search with tineye
https://www.tineye.com/search/153d902d2e4567ccb3299daefa3cef8d207d197a/

or google image search
https://www.google.com/search?tbs=sbi:AMhZZiua3avdA9z9KnzBOe4pBpsmp-1LJjdEXd13gP1bdXWtunUl2CB6caY5wjn56t8GA8l9KNMqKZdLYHBYPpAuwanPvVp6nJImULD5vgQ9FtisQkTSb5t6Cme58vhCq8Ui2VhStHnEXzHkr4EOgy_1y35oGW4pkLBRc4gQdYYazjC8AR3gqBGoBcwWrxAg7Jnytas9YRdy12rrY4OGg9UnShQgqJSNjDJVnjdsIrzevtFAF0hVY0yKBKahxLAY8lxwjWrYu_1hPB7aY8Il_11RYWHT32QuTvvd3kM943QUxMlQox0zmyMsB0NCuzyJzNkOrhm9lfDf_1k9HpikGcP-m_1wIUF5AWmbznw=1878=1260=search=X=0ahUKEwi4_Z-56cXhAhUSQq0KHUHGCtcQ9Q8IJCgA

to find more versions of the image.
Regards,
Mitch

Quoting Jonathan Davies :


See below:

https://www.nature.com/articles/449144a

--
Jonathan Davies, PhD
Postdoctoral Researcher, Stenmark Lab
Department of Biochemistry and Biophysics
Stockholm University
Sweden







On 10 Apr 2019, at 16:29, Zachary A. Wood  
mailto:z...@uga.edu>> wrote:


Hello Fellow Structural Enthusiasts,

My apologies for the slightly off-topic question. I am trying to  
track down a higher resolution image of the jpg that I have  
attached. I use this photo of Max Perutz when I am teaching about  
protein folding, and have always wanted a better quality one. I  
believe it is credited to Nature, and I am trying to find out what  
issue, but I am hoping that one of you may have more information or  
perhaps even a better photo. Thanks for any help, and for those of  
you who may never have seen this photo before, I hope you enjoy it.  
I like to imagine that Perutz is considering the challenges  
associated with folding that chain after he determined the crystal  
structure. If you have never read the discussion in his famous  
Nature paper, I will leave you with a relevant quote of him  
referring to the structural similarity between horse hemoglobin and  
sperm whale myoglobin, in which he predicts the thermodynamic  
hypothesis (Anfinsen’s dogma):


“How does this arise? It is scarcely conceivable that a  
three-dimensional template forces the chain to take up this fold.  
More probably, the chain, once synthesized and provided with a haem  
group around which it can coil, takes up this configuration  
spontaneously, as the only one which satisfies the stereochemical  
requirements of its amino acid sequence.”


Thank you for any help you may be able to offer!

Best regards,

Z

***
Zachary A. Wood, Ph.D.
Associate Professor and Graduate Coordinator
Department of Biochemistry & Molecular Biology
University of Georgia
Life Sciences Building, Rm A426B
120 Green Street
Athens, GA  30602-7229
Office: 706-583-0304
Lab:706-583-0303
FAX: 706-542-1738
***




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Re: [ccp4bb] A Max Perutz question

[Savvas Savvides]

Hey Zac
A good scan of page 228 in Georgina Ferry’s biography of Max Perutx (Max Perutz 
and the secret of life) will do the trick. It is a 18x13 cm photo. I have it in 
front of me!

best 
Savvas

> On 10 Apr 2019, at 16:29, Zachary A. Wood  wrote:
> 
> Hello Fellow Structural Enthusiasts,
> 
> My apologies for the slightly off-topic question. I am trying to track down a 
> higher resolution image of the jpg that I have attached. I use this photo of 
> Max Perutz when I am teaching about protein folding, and have always wanted a 
> better quality one. I believe it is credited to Nature, and I am trying to 
> find out what issue, but I am hoping that one of you may have more 
> information or perhaps even a better photo. Thanks for any help, and for 
> those of you who may never have seen this photo before, I hope you enjoy it. 
> I like to imagine that Perutz is considering the challenges associated with 
> folding that chain after he determined the crystal structure. If you have 
> never read the discussion in his famous Nature paper, I will leave you with a 
> relevant quote of him referring to the structural similarity between horse 
> hemoglobin and sperm whale myoglobin, in which he predicts the thermodynamic 
> hypothesis (Anfinsen’s dogma):
> 
> “How does this arise? It is scarcely conceivable that a three-dimensional 
> template forces the chain to take up this fold. More probably, the chain, 
> once synthesized and provided with a haem group around which it can coil, 
> takes up this configuration spontaneously, as the only one which satisfies 
> the stereochemical requirements of its amino acid sequence.” 
> 
> Thank you for any help you may be able to offer!
> 
>  Best regards,
> 
> Z
> 
> ***
> Zachary A. Wood, Ph.D.
> Associate Professor and Graduate Coordinator  
> Department of Biochemistry & Molecular Biology
> University of Georgia
> Life Sciences Building, Rm A426B
> 120 Green Street
> Athens, GA  30602-7229
> Office: 706-583-0304
> Lab:706-583-0303
> FAX: 706-542-1738
> ***
> 
> 
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1 
> 



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Re: [ccp4bb] A Max Perutz question

[Jonathan Davies]

See below:

https://www.nature.com/articles/449144a

--
Jonathan Davies, PhD
Postdoctoral Researcher, Stenmark Lab
Department of Biochemistry and Biophysics
Stockholm University
Sweden







On 10 Apr 2019, at 16:29, Zachary A. Wood mailto:z...@uga.edu>> 
wrote:

Hello Fellow Structural Enthusiasts,

My apologies for the slightly off-topic question. I am trying to track down a 
higher resolution image of the jpg that I have attached. I use this photo of 
Max Perutz when I am teaching about protein folding, and have always wanted a 
better quality one. I believe it is credited to Nature, and I am trying to find 
out what issue, but I am hoping that one of you may have more information or 
perhaps even a better photo. Thanks for any help, and for those of you who may 
never have seen this photo before, I hope you enjoy it. I like to imagine that 
Perutz is considering the challenges associated with folding that chain after 
he determined the crystal structure. If you have never read the discussion in 
his famous Nature paper, I will leave you with a relevant quote of him 
referring to the structural similarity between horse hemoglobin and sperm whale 
myoglobin, in which he predicts the thermodynamic hypothesis (Anfinsen’s dogma):

“How does this arise? It is scarcely conceivable that a three-dimensional 
template forces the chain to take up this fold. More probably, the chain, once 
synthesized and provided with a haem group around which it can coil, takes up 
this configuration spontaneously, as the only one which satisfies the 
stereochemical requirements of its amino acid sequence.”

Thank you for any help you may be able to offer!

 Best regards,

Z

***
Zachary A. Wood, Ph.D.
Associate Professor and Graduate Coordinator
Department of Biochemistry & Molecular Biology
University of Georgia
Life Sciences Building, Rm A426B
120 Green Street
Athens, GA  30602-7229
Office: 706-583-0304
Lab:706-583-0303
FAX: 706-542-1738
***




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Re: [ccp4bb] A Max Perutz question

[Bonsor, Daniel]

https://www.nature.com/articles/449144a

Daniel A Bonsor PhD.
Sundberg Lab
Institute of Human Virology
University of Maryland, Baltimore
725 W Lombard Street N370
Baltimore
Maryland
MD 21201
Tel: (410) 706-7457


From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Zachary 
A. Wood
Sent: Wednesday, April 10, 2019 10:30 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] A Max Perutz question

Hello Fellow Structural Enthusiasts,

My apologies for the slightly off-topic question. I am trying to track down a 
higher resolution image of the jpg that I have attached. I use this photo of 
Max Perutz when I am teaching about protein folding, and have always wanted a 
better quality one. I believe it is credited to Nature, and I am trying to find 
out what issue, but I am hoping that one of you may have more information or 
perhaps even a better photo. Thanks for any help, and for those of you who may 
never have seen this photo before, I hope you enjoy it. I like to imagine that 
Perutz is considering the challenges associated with folding that chain after 
he determined the crystal structure. If you have never read the discussion in 
his famous Nature paper, I will leave you with a relevant quote of him 
referring to the structural similarity between horse hemoglobin and sperm whale 
myoglobin, in which he predicts the thermodynamic hypothesis (Anfinsen’s dogma):

“How does this arise? It is scarcely conceivable that a three-dimensional 
template forces the chain to take up this fold. More probably, the chain, once 
synthesized and provided with a haem group around which it can coil, takes up 
this configuration spontaneously, as the only one which satisfies the 
stereochemical requirements of its amino acid sequence.”

Thank you for any help you may be able to offer!

 Best regards,

Z

***
Zachary A. Wood, Ph.D.
Associate Professor and Graduate Coordinator
Department of Biochemistry & Molecular Biology
University of Georgia
Life Sciences Building, Rm A426B
120 Green Street
Athens, GA  30602-7229
Office: 706-583-0304
Lab:706-583-0303
FAX: 706-542-1738
***
[cid:image001.jpg@01D4EF89.4B618FB0]



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[ccp4bb] A Max Perutz question

[Zachary A. Wood]

Hello Fellow Structural Enthusiasts,

My apologies for the slightly off-topic question. I am trying to track down a 
higher resolution image of the jpg that I have attached. I use this photo of 
Max Perutz when I am teaching about protein folding, and have always wanted a 
better quality one. I believe it is credited to Nature, and I am trying to find 
out what issue, but I am hoping that one of you may have more information or 
perhaps even a better photo. Thanks for any help, and for those of you who may 
never have seen this photo before, I hope you enjoy it. I like to imagine that 
Perutz is considering the challenges associated with folding that chain after 
he determined the crystal structure. If you have never read the discussion in 
his famous Nature paper, I will leave you with a relevant quote of him 
referring to the structural similarity between horse hemoglobin and sperm whale 
myoglobin, in which he predicts the thermodynamic hypothesis (Anfinsen’s dogma):

“How does this arise? It is scarcely conceivable that a three-dimensional 
template forces the chain to take up this fold. More probably, the chain, once 
synthesized and provided with a haem group around which it can coil, takes up 
this configuration spontaneously, as the only one which satisfies the 
stereochemical requirements of its amino acid sequence.”

Thank you for any help you may be able to offer!

 Best regards,

Z

***
Zachary A. Wood, Ph.D.
Associate Professor and Graduate Coordinator
Department of Biochemistry & Molecular Biology
University of Georgia
Life Sciences Building, Rm A426B
120 Green Street
Athens, GA  30602-7229
Office: 706-583-0304
Lab:706-583-0303
FAX: 706-542-1738
***
[cid:442ED6C1-8442-400E-9156-C7C062ABC0EC]



To unsubscribe from the CCP4BB list, click the following link:
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