Thanks Randy,

so from your reply it seems that cutoff is differently treated. And if I 
interpret your email correctly it is better to provide Phaser with a truncated 
versus a full data set. I tried both cases, but I had assumed that if you 
restrict the resolution within Phaser it would be the same as if you give 
Phaser to begin with a truncated dataset.
Perhaps it would be a good idea in th automatic routine to first check if the 
user wants to truncate the data and then run the automatic scoring analysis 
with that value ?

Jürgen

......................
Jürgen Bosch
Johns Hopkins University
Bloomberg School of Public Health
Department of Biochemistry & Molecular Biology
Johns Hopkins Malaria Research Institute
615 North Wolfe Street, W8708
Baltimore, MD 21205
Office: +1-410-614-4742<tel:%2B1-410-614-4742>
Lab:      +1-410-614-4894<tel:%2B1-410-614-4894>
Fax:      +1-410-955-2926<tel:%2B1-410-955-2926>
http://lupo.jhsph.edu

On Oct 1, 2014, at 5:15 AM, Randy Read 
<[email protected]<mailto:[email protected]>> wrote:

Hi Jurgen,

You could send me a logfile off-list, and maybe I would spot something in there.

We’ve put some effort into putting more intelligence into the Phaser search, so 
that it adapts to the initial perceived difficulty of the problem in setting 
the initial parameters, and then adapts to indicators of success or failure 
during the search.  Much of the time this works very well, but there’s 
obviously room for improvement.  For one thing, it appears that we’re 
frequently too optimistic about how good the model will be and how easy the 
search will be.

One question: when you say that you cut at 2.5A for MR, do you do that by 
setting the resolution within the Phaser run, or do you have an MTZ file with 
only data to 2.5A?  If the former, then you’re over-riding some of Phaser’s 
automation, which will choose the initial resolution limit based on the 
perceived difficulty of the problem (a function of model completeness, expected 
RMS error of the model, and the number of reflections to different resolution 
limits).  It’s this initial automated choice that can go wrong if we’re too 
optimistic, because then a clear solution isn’t found, and then Phaser repeats 
the search with data to the full resolution, which can take longer than just 
choosing an intermediate resolution from the start.

Anyway, if the problem is expected to be easy but turns out to be difficult, 
this implies that some of the information used to decide it should be easy is 
wrong or too optimistic.  One top possibility is that the model is not as good 
as expected, e.g. because of conformational changes.  If there’s a potential 
hinge-bending motion, then you’re usually better off searching with separate 
domains.  If the change is something that can’t be described with rigid-body 
motions, then it would be better to increase the expected RMS error from what 
Phaser deduces from the sequence identity.  Increasing the RMSD by 10-20% would 
be a good first bet in such a case.

The other top possibility is that the space group is wrong.  Is there any 
ambiguity in the space group?  In particular, do any of the twinning tests 
indicate that the data may be twinned (which can lead to choosing too high 
symmetry)?

Best wishes,

Randy

On 1 Oct 2014, at 03:02, Jurgen Bosch <[email protected]<mailto:[email protected]>> 
wrote:

Dear BB, or in particular Phaser developers :-)

This must be part of British humor right (or was that the Canadian influence 
Randy) ?

eLLG indicates that placement of ensemble "ensemble_1" will be straightforward
   The data are sufficient to exceed the eLLG target

The search space is finite 143 x 143 x 80 Å with 3 or 4 molecules per asu, but 
Phaser has been burning CPU cycles quite a bit, we are approaching 24h by now. 
Data extends to 1.7 Å - for MR we cut at 2.5 Å.

I can hear Garib, yes, Molrep was done in few minutes but I’m not super 
convinced about the solution either. Same with BALBES and MrBump (which took a 
few more minutes, actually also days for MrBump)

The space group appears to be P63 22 as judged by XDS, pointless, xtriage, 
however the crystals are split (at least in some areas it’s visible) but I 
thought XDS would take care of these “aliens” and eliminate them mostly. My 
graduate student, Lauren, found a nifty program called DIALS that we wish to 
explore further to rescue the “nice” data we have and hopefully solve the 
structure.

Lower symmetry space groups were tried down to P21 with increasing number of 
molecules per asu and applying twin laws if necessary. The minor problem with 
the twins is how do I really know that it is a higher symmetry space group and 
not a 50% twin in a lower symmetry ? Rwork/Rfree in this particular case do not 
seem to help at all for distinguishing between the solutions. Maps looks sort 
of right but R-factors are not reflecting what you see on the screen.

We appreciate any suggestions and ideas what else we could do.

Thanks,

Jürgen

......................
Jürgen Bosch
Johns Hopkins University
Bloomberg School of Public Health
Department of Biochemistry & Molecular Biology
Johns Hopkins Malaria Research Institute
615 North Wolfe Street, W8708
Baltimore, MD 21205
Office: +1-410-614-4742<tel:%2B1-410-614-4742>
Lab:      +1-410-614-4894<tel:%2B1-410-614-4894>
Fax:      +1-410-955-2926<tel:%2B1-410-955-2926>
http://lupo.jhsph.edu<http://lupo.jhsph.edu/>


------
Randy J. Read
Department of Haematology, University of Cambridge
Cambridge Institute for Medical Research      Tel: + 44 1223 336500
Wellcome Trust/MRC Building                   Fax: + 44 1223 336827
Hills Road                                    E-mail: 
[email protected]<mailto:[email protected]>
Cambridge CB2 0XY, U.K.                       www-structmed.cimr.cam.ac.uk


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