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This article may be informative:

Nat Struct Biol. 2003 Mar;10(3):219-25. 

Extensive conformational sampling in a ternary electron transfer complex.
Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS.

They describe a structure of a protein-protein complex in which one large
piece is disordered.



> From: Song Tan <[EMAIL PROTECTED]>
> Date: Tue, 3 Oct 2006 09:02:39 -0400
> To: shivesh kumar <[EMAIL PROTECTED]>, <ccp4bb@dl.ac.uk>
> Subject: Re: [ccp4bb]: half of the structure missing
> 
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> 
> 
> Others have made excellent comments and suggestions.  I would also
> offer the following precedent:
> 
> Loris et al, JBC, 278:28252, 2003 where electron density of only half
> of the MazE protein was detected, with the rest of the 82 aa protein
> disordered but present in the crystal.
> 
> The structure of the MazE/MazF complex showed that the remaining half
> of MazE formed an extended chain that cofolded with the MazF partner
> (Kamada et al, Mol Cell, 11:875, 2003).  In the absence of MazF, this
> half of MazE would not fold, consistent with the absence of defined
> structure in the MazE/antibody cocrystal structure.
> 
> Regards,
> 
> Song
> 
> 
>> Dear all,
>> At present we have 2.4A resolution.the protein is supposed to have
>> two domains separated by a 8-residues linker region with 3 glycines
>> which we have checked with DisEMBL.So,one domain is can be
>> flexible.We have done the mass spectroscopy of the protein solution
>> itself and we are trying to check with the crystals also.There is no
>> tag in the protein.We kept two acetate molecules and 13 water
>> molecules and it has two bound calciums.
>> ThanX in advance.
>> shivesh
> 
> 
> -- 
> 
> Dr. Song Tan
> Associate Professor in Biochemistry & Molecular Biology
> Center for Gene Regulation
> Dept of Biochemistry & Molecular Biology
> 108 Althouse Laboratory   (office & lab in 3 Althouse Laboratory)
> Penn State University
> University Park, PA   16802
> email:  [EMAIL PROTECTED]    http://www.bmb.psu.edu/faculty/tan/lab/
> phone:  814-865-3355     fax: 814-863-7024


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