Dear Thuy,

For blob1 you should also try to fit alternative conformations. Your maps are 
good enough to give you a fair chance. You should also look for reasons behind 
these alternative conformations: has a neighboring disulfide bond partially 
opened? Is there a partially-occupied cadmium nearby? Is the substrate 
partially converted into product? Etc. From the static pictures without the 
neighborhood, we cannot deduce this for you.

Best,
Herman

Von: CCP4 bulletin board [mailto:[email protected]] Im Auftrag von thuy ngo
Gesendet: Donnerstag, 31. Oktober 2013 10:05
An: [email protected]
Betreff: Re: [ccp4bb] help with strange density map

Dear all,

The gly104 sequence is correct. This is the substrate complex structure. In 
case of native structure, such strange of blob1 didnot appear
Also for the second blob, I follow your suggestion and the result is nice
I am still waitting for the suggestion of the first blob

Thank you a lot,
Sincerely yours

On Thursday, October 31, 2013 4:45 PM, Prof. Dr. Arne Skerra 
<[email protected]<mailto:[email protected]>> wrote:
Can you exclude a sequencing error for Gly104?

Am 31.10.2013 um 08:40 schrieb thuy ngo:


Dear all,

I am dealing with two strange extra density map. One is connected from Cb of 
Proline to Ca of glycine (blob 1)
 and other is positioned between two symmetric molecules which is connected 
from Cb of Histidine to carboxylate group of Glutamate. I checked all the 
crystallization and purification condition but no ligand is suitable for these 
blobs. Could you suggest some possible candidates?
This is the structure complex between peptide deformylase and fMAS
Crystallization condition: 2M Sodium acetate, 0.1 M HEPES 7.5 and 0.05M CdSO4

Thank you
<blob1_back.png><blob1_front.png><blob2.png>


Prof. Dr. Arne Skerra
Lehrstuhl f. Biologische Chemie  |  Technische Universitaet Muenchen
Emil-Erlenmeyer-Forum 5  |  85350 Freising-Weihenstephan  |  Germany
Phone: +49 (0)8161 71-4351  |  Fax: -4352
eMail: [email protected]<mailto:[email protected]>  |  http://www.wzw.tum.de/bc




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