[ccp4bb] size of protein in negatively stained TEM?

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CCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999

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Subject: Re: Catalytic residues in active sites
From: Donnie Berkholz dberkholz {- at -} GENTOO {- dot -} ORG
Date: 2010-05-28

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From: Christine Bentz Christine {- dot -} Bentz {- at -} HELMHOLTZ-HZI {- dot -} DE
Date: 2010-05-28

Subject: size of protein in negatively stained TEM?
From: Chad K Park ckpark {- at -} EMAIL {- dot -} ARIZONA {- dot -} EDU
Date: 2010-05-28

Apologies for the non-crystallographic question, but I would think the wide
experience and vitality of this board might have some opinions on this
topic.

We've sent out some samples for negative staining electron microscopy. They
were stained with uranyl acetate on commercial grids and the resulting
images seem to have a dispersity in the size of the little round blobs seen.
Some of the blobs look like they might be what we see in our crystal
structures. However, some of them are quite large. What have people's
experience been with this technique and how close you get to an overall
dimension for your protein or complex? How closely has that number been to
results from other techniques (Xtallography, DLS, other hydrodynamic methods
....)? Is there some rule of thumb that describes if the image is slightly
smaller or larger than the expected size?

Thanks for your comments.

Regards,
Chad K. Park,
Analyt. Biophys. Core
Chem./Biochem., U. of AZ

CCP4bb navigation

CCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999

Previous message:
Subject: Re: Catalytic residues in active sites
From: Donnie Berkholz dberkholz {- at -} GENTOO {- dot -} ORG
Date: 2010-05-28

Next message:
Subject: Job Advertisment (PhD position)
From: Christine Bentz Christine {- dot -} Bentz {- at -} HELMHOLTZ-HZI {- dot -} DE
Date: 2010-05-28