Along the lines of Roger's second point, there was a very nice paper a few 
years back that found very good agreement between the conformational ensemble 
sampled by ubiquitin in solution (by NMR) with the ensemble of conformations 
observed in a large number of crystal structures:

Lange OF, Lakomek NA, Farès C, Schröder GF, Walter KF, Becker S, Meiler J, 
Grubmüller H, Griesinger C, de Groot BL.
Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin 
ensemble in solution.
Science. 2008 Jun 13;320(5882):1471-5. PubMed PMID: 18556554.

Best,

Damian Ekiert


On Feb 10, 2012, at 12:50 PM, Roger Rowlett wrote:

> I believe the most justifiable assumption one can make is that crystal 
> structures are likely to represent the least soluble conformations of a 
> protein under the conditions of crystallization (which might be a broad range 
> of conditions, including physiological). This can be quite vexing if you are 
> studying an allosteric protein and one of the two conformations is typically 
> much less soluble than the other. BTDT. I'm sure others have had the same 
> experience.
> 
> Having said that, the solvent content of protein crystals (which is close to 
> that of cellular conditions), the observation of enzymatic activity in many 
> protein crystals, and the *general* concordance of XRD and NMR structures of 
> proteins (when both have been determined) leads one to believe that XRD 
> structures are likely representative of physiologically relevant 
> conformations.
> 
> Cheers,
> 
> _______________________________________
> Roger S. Rowlett
> Gordon & Dorothy Kline Professor
> Department of Chemistry
> Colgate University
> 13 Oak Drive
> Hamilton, NY 13346
> 
> tel: (315)-228-7245
> ofc: (315)-228-7395
> fax: (315)-228-7935
> email: [email protected]
> 
> On 2/10/2012 3:34 PM, Nat Echols wrote:
>> On Fri, Feb 10, 2012 at 12:29 PM, James Stroud <[email protected]>
>>  wrote:
>> 
>>> How could they not be snapshots of conformations adopted in solution?
>>> 
>> Packing billions of copies of an irregularly-shaped protein into a
>> compact lattice and freezing it to 100K isn't necessarily
>> representative of "solution", especially when your solution contains
>> non-physiological amounts of salt and various organics (and possibly
>> non-physiological pH too).
>> 
>> -Nat
>> 

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