Hello,
I rather think the model has a problem.
Are there large domains which are invisible in the structure ?
Is it possible that the data are twinned ?
Did you use TLS refinement to account for anisotropy ?
Just cutting the resolution will probably not help, unless there is a serious problem in data quality.
Best
Wim

On 25/03/2019 13:31, Sharan Karade wrote:
As I understand helical assembly, the data some time is anisotropic (any one or two a*,b* or c* has more diffraction than other), which may be responsible for your high Rfactors. You can crop the data to the resolution using softwares.

Regards
Sharan

On Mon, Mar 25, 2019, 8:17 AM Andreas Förster <docandr...@gmail.com> wrote:
Yeah, good stuff:


All best.


Andreas



On Mon, Mar 25, 2019 at 10:45 AM CCP4BB <0000193323b1e616-dmarc-requ...@jiscmail.ac.uk> wrote:
Even if you can't see them, it may be worthwhile investigating with Auspex (Parkhurst, Thorn, Winter & Waterman - sorry, I can't remember the reference off-hand). There's an easy to use webserver somewhere that runs it...

Harry
--
Dr Harry Powell

On 25 Mar 2019, at 09:03, herman.schreu...@sanofi.com wrote:

Dear ???,

Do you have any ice rings (even hardly visible ones) in your diffraction data?

Best,

Herman

 

Von: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] Im Auftrag von StrBio
Gesendet: Sonntag, 24. März 2019 05:17
An: CCP4BB@JISCMAIL.AC.UK
Betreff: [EXTERNAL] [ccp4bb] Refinement

 

ALL.

 

I have data at 2.4 A in P21 sp gr, helical protein.

Refined to Rwork 29 Rfree 34 with nice density map and all nice statistics oither Rfactor (by Phenix). Refmac quit same.

Should I deposit it or look better data?

Any suggestion?

 

 

 


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