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I222 and P2(1)2(1)2 are closely related.  Change one of the
crystallographic two-folds into a non-crystallographic two-fold and
Bob's your uncle.

Demetallized Concanavalin A crystallizes in P2(1)2(1)2.  Add cations to
the crystals and they'll change into the same form (I222) that you get
by crystallizing the metallo-protein directly.  See Becker et al. (1975)
JBC 250:1513 and Reeke et al. (1978) PNAS 75:2286.

Joe Becker
Merck Research Labs

-----Original Message-----
From: [EMAIL PROTECTED] [mailto:[EMAIL PROTECTED] On Behalf Of
Zorg Blue
Sent: Wednesday, November 08, 2006 2:58 AM
To: [email protected]
Subject: [ccp4bb]: Pseudosymmetry and free R sets

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Hello,

We have solved the structure of a protein that crystallised in space
group 
I222 with 1 molecule per asymmetric unit. After refining the structure
to 
3.5 A, we obtained a different crystal form that diffracts to higher 
resolution; in this case, the space group appears to be P21212, with the

same unit cell as the first type of crystals and 2 molecules per
asymmetric 
unit. The packing between the two molecules in the P21212 asymmetric
unit is 
identical to that of symmetry-related molecules in the I222 crystals, 
suggesting that the space group of crystal form 1 could also be P21212,
with 
non-crystallographic symmetry giving rise to strong pseudo-I222 symmetry
at 
low resolution.

Since we have already refined our model against the low resolution data 
processed in I222, what would be the best way to define a new free R set
in 
order to continue refinement against the higher resolution P21212 data?
If 
our interpretation is correct, I would think that using a completely new
set 
would introduce some bias; on the other hand, is there any way to
somehow 
take into account the pseudo-symmetry we observe?

Thank you for any advice,

Zorg

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