ob Keller
> Sent: Thursday, 16 February 2012 7:36 a.m.
> To: CCP4BB@JISCMAIL.AC.UK
> Subject: Re: [ccp4bb] surface residue mutation
>
> Right on the money!
>
> JPK
>
> On Wed, Feb 15, 2012 at 12:28 PM, David Schuller
> wrote:
> > On 02/15/12 12:41, Jacob Keller wro
Jacob
Keller
Sent: Thursday, 16 February 2012 7:36 a.m.
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] surface residue mutation
Right on the money!
JPK
On Wed, Feb 15, 2012 at 12:28 PM, David Schuller wrote:
> On 02/15/12 12:41, Jacob Keller wrote:
>>>
>>> Are there any all
Right on the money!
JPK
On Wed, Feb 15, 2012 at 12:28 PM, David Schuller wrote:
> On 02/15/12 12:41, Jacob Keller wrote:
>>>
>>> Are there any all-D proteins out there, of known structure or
>>> otherwise? If so, do enantiomer-specific catalyses become inverted?
>>>
>>> JPK
>>>
> I looked a lit
On 02/15/12 12:41, Jacob Keller wrote:
Are there any all-D proteins out there, of known structure or
otherwise? If so, do enantiomer-specific catalyses become inverted?
JPK
I looked a little harder, and at least one D-enantiomeric protein was an
enzyme:
Total chemical synthesis of a D-enzym
On 02/15/12 12:41, Jacob Keller wrote:
Are there any all-D proteins out there, of known structure or
otherwise? If so, do enantiomer-specific catalyses become inverted?
JPK
What do you mean by "Out There"? If you mean in the PDB, then yes. As
of two weeks ago, there are ~ 14 racemic structures
bject: [ccp4bb] AW: [ccp4bb] surface residue mutation
Hi Prem,
besides trying surface entropy reduction you can also start by analyzing your
crystal contacts and mutate residues therein. This was for example
investigated in the 90's by GE Schulz and coworkers.
Good Luck
Alex
The most famous case I know of was the HIV protease. My grad school PI used
to use it as an example in class.
Science. 1992 Jun 5;256(5062):1445-8.
Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease
show reciprocal chiral substrate specificity [corrected].
Milton RC, Milton
Are there any all-D proteins out there, of known structure or
otherwise? If so, do enantiomer-specific catalyses become inverted?
JPK
On Wed, Feb 15, 2012 at 8:05 AM, David Schuller wrote:
> Wukovitz & Yeates (1995) Nature Struc. Biol. 2(12): 1062-1067
> predicts that the most probable space gro
Wukovitz & Yeates (1995) Nature Struc. Biol. 2(12): 1062-1067
predicts that the most probable space group for macromolecular
crystallization is P -1 (P 1-bar). All you have to do to try it out is
synthesize the all-D enantiomer of your protein and get it to fold properly.
On 02/14/12 18:36, Pr
/
but no space group predictions are possible. BR
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of
Prem
Kaushal
Sent: Tuesday, February 14, 2012 3:36 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] surface residue mutation
Hi
We have a protein that crystallized in
horized review, use, disclosure, copying or
distribution is strictly prohibited.
Von: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] Im Auftrag von Prem
Kaushal
Gesendet: Mittwoch, 15. Februar 2012 00:36
An: CCP4BB@JISCMAIL.AC.UK
Betreff: [ccp4bb] surface residue mutation
Hi
We have a protein t
Have you solved the structure? It's just that you don't say why you need
different crystal forms.
We had to do a bit of "crystal engineering" in order to get a complex between
our protein and a peptide. It turned out to be relatively simple case; visually
inspecting the crystal packing (in Coot
http://services.mbi.ucla.edu/SER/
but no space group predictions are possible. BR
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Prem
Kaushal
Sent: Tuesday, February 14, 2012 3:36 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] surface residue mutation
Hi
Hi
We have a protein that crystallized in P21212 space group. We are looking
for some different crystal forms. We tried few things did not work. Now we
are thinking to mutate surface residues. Anybody aware of any software
which can predict the mutations that might help in crystallizing protein in
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