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Personally, I have found that His-SELECT from Sigma appears to have the
lowest contaminant binding of the IMAC resins that I've compared. Presumably
this is due to the mostly hydrophilic nature of the linker (as compared to
mostly hydrophobic linkers of other resins). Note that I have no association
with Sigma or any other equipment/supplies manufacturer.

As far as flow rates etc. - if you have access to a decent purification
workstation (such as any of the AKTA series, or a Biocad [the latter is not
supported any more]) - flow rate becomes primarlily dependent on the maximum
back pressure recommended by the manufacturer of the resin and the column in
which it is poured. Short and fat columns perform better in this regard than
long & thin ones, obviously.

Highly crosslinked sepharose has decent flow rates and decent pressure
characteristics. I routinely run these types of columns at 1 MPa even though
manufacturers typically recommend 0.4-0.6 MPa maximum. I believe that Poros
media has much higher pressure limit. High-pressure columns tend to be more
expensive than lower-pressure ones, of course.

If you do not have access to purification equipment capable of
medium-pressure chromatography, or if you must resort to multiple
gravity-driven columns for parallel work, then batch binding may be an
optimum solution. Detergent lysis *without* lysozyme is often better for
this kind of work as there's less cell debris generated. Adding DNAse or
bensonase to the lysate (even if you French press or sonicate) will reduce
your viscosity considerably, as will the extended centrifugation (such as
1hr spin at 20,000 rcf or better). You can 'assist' gravity columns with
gentle pressure of air provided that you have liquid in the reservoir so the
column never dries up.

Artem

-----Original Message-----
From: [EMAIL PROTECTED] [mailto:[EMAIL PROTECTED] On Behalf Of Nat
Echols
Sent: Sunday, October 08, 2006 2:11 AM
To: [email protected]
Subject: [ccp4bb]: off-topic: Ni purification media

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This is indirectly crystallization-related:

Can anyone comment on the usefulness of Poros MC resin for purification of 
His-tagged proteins, especially in comparison to the various Amersham 
products?  I'm dealing with a protein that is happiest with 20% glycerol 
in the initial buffer, and this makes any FPLC- or pump-based purification 
very slow due to the relatively low pressure tolerance of Sepharose 
media.  The Poros ion exchange resin works very well and is both robust 
and cheap, but the MC resin is about 5 times more expensive than anything 
else I've found.  Other than the price, is there any reason not to use 
it?

(For what it's worth, batch purification with Sepharose works relatively 
well for me, but I've found it too cumbersome in practice and I'm trying 
to scale up with multiple constructs in this particular case.)

thanks,
Nat

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