York
Department of Chemistry, MR-1135
160 Convent Avenue
New York, NY 10031
Tel. (212) 650-6070
www.khayatlab.org
Original message
>Date: Sat, 20 Dec 2014 10:44:25 -0800
>From: CCP4 bulletin board (on
behalf of Christine Gee )
>Subject: Re: [ccp4bb] non-specific disulfide
Hello Todd,
if your protein is a cytosolic protein (reductive environment; for ER,
Golgi, mitochondria things look different), the disulfide bond formation
you observe is most probably the result of the oxidative environment
(outside the cell) in combination with the crystal packing that that
, MR-1135
160 Convent Avenue
New York, NY 10031
Tel. (212) 650-6070
www.khayatlab.org
Original message
>Date: Sat, 20 Dec 2014 10:44:25 -0800
>From: CCP4 bulletin board (on
behalf of Christine Gee )
>Subject: Re: [ccp4bb] non-specific disulfide bonds in
crystal structu
Hi Todd,
I used to work on PNMT which also is supposedly monomeric and formed a
disulfide between monomers in the crystals. See
http://www.sciencedirect.com/science/article/pii/S1570963905000968?via=ihub
We showed that it was irrelevant to activity.
Cheers
Christine
Sent from my iPad
> On 20
Hello All-
I have recently determined a domain structure of a larger protein. The
structure shows a clear disulfide bond between two monomers in the asymmetric
unit. I'm trying to figure out if this is an artifact of the crystal packing or
has biological relevance. The protein has been reported
