Refining B-aniso's will clean up a difference map at that resolution.
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On Tue, 9 Jul 2019 at 16:57, Bonsor, Daniel<dbon...@som.umaryland.edu> wrote:
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Have you mass-speced the protein before crystallization to make sure it wasn’t
derivatized during expression and/or purification, or compared the mass spec of
the crystals verses purified protein? Any fancy reagents or other reductants
used during purification?
What about S-Acetyl-cysteine (3-letter code: SCY).
Best,
Dan
Daniel A Bonsor PhD.
Sundberg Lab
Institute of Human Virology
University of Maryland, Baltimore
725 W Lombard Street N370
Baltimore
Maryland
MD 21201
Tel: (410) 706-7457
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK]On Behalf Of Lumbini
Yadav
Sent: Tuesday, July 09, 2019 5:22 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Fo-Fc density close to cysteine residue
Dear all,
We have found a huge Fo-Fc density close to cysteine residue (see attached
image) in the structure with resolution of 1.2A. In the crystallization
condition, we have PEG 3350, Potassium phosphate monobasic, glycerol and
protein was in Tris and NaCl. Before freezing the crystals were soaked in
mother liquor containing sodium dithionite.
I have tried different modified cysteine (CSX, CSO, OCS, CME, CSS, SNC, CSD,
CXM, SCH, CSU) from the library and also SO3, SO2 and peroxide. But in all the
screenings we do see some part of Fo-Fc density unaddressed at 3 sigma.
Does anyone have an idea about what this density could be? Covalent
modification?
Thanks.
Kind regards,
Lumbini
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