Petegem [mailto:[EMAIL PROTECTED]
Envoyé : Monday, June 30, 2008 9:01 PM
À : Philippe DUMAS
Cc : CCP4BB@jiscmail.ac.uk
Objet : Re: [ccp4bb] Weakest protein-protein complex crystallised
Hi,
we've had a similar situation: a protein-peptide complex with a Kd in the
nM range crystallized in the same
I hope this isn't too much of a foray into philosophy and semantics,
but can't you argue that the crystals themselves are weak complexes?
And since the energies of crystal contacts are typically very weak, I
would further argue that you should be able to crystallize ANY
complex with an
The word weak is, of course, relative. Free energy of crystallization
is roughly 1-2 kcal/mole of crystal contacts (I think I carried this
number from Sir Blundell's book, but quick look at papers by Peter
Vekilov's group seems to confirm it - am I wrong on this?). I think
that crystal contacts
There are quite a number of structures homodimers and homotetramers in the PDB
where the dissociation constant is known to be in the millimolar range.
For example the dimerizaion of a humainized antibody VHH domain that mimicks a
VH-VL complex (Conrath et al. J. Mol. Biol. (2005) 350, 112125).
Descartes 67084 Strasbourg cedex
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-Message d'origine-
De : CCP4 bulletin board [mailto:[EMAIL PROTECTED] la part de Ed
Pozharski
Envoyé : Monday, June 30, 2008 4:50 PM
À : CCP4BB@JISCMAIL.AC.UK
Objet : Re: [ccp4bb] Weakest protein-protein
] Weakest protein-protein complex crystallised
The word weak is, of course, relative. Free energy of crystallization
is roughly 1-2 kcal/mole of crystal contacts (I think I carried this
number from Sir Blundell's book, but quick look at papers by Peter
Vekilov's group seems to confirm
@JISCMAIL.AC.UK
Objet : Re: [ccp4bb] Weakest protein-protein complex crystallised
The word weak is, of course, relative. Free energy of
crystallization
is roughly 1-2 kcal/mole of crystal contacts (I think I carried this
number from Sir Blundell's book, but quick look at papers by Peter
Hello John,
No, they're not. Crystals were obtained at pH8.0, 200mM NaCl; 10%
PEG4000. Calorimetric experiments were done at pH7.4, 150mM KCl. We found
the interaction to be driven mainly by hydrophobic contacts (mutants of
polar/charged residues have no significant effect on the affinity).
