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Hi Vincent,<br>
<br>
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cite="mid:eb10968d-120c-9097-301c-de5469c78e52@ibcp.fr">
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<font size="+1"><tt>I am very lucky to see 2 maps of the same
protein, at roughly the same resolution, one by Xray and the
other by EM (it's not that common). The details from the 2
maps are however different... <br>
</tt></font></blockquote>
<br>
<tt><font size="+1">wow, fascinating! <br>
<br>
</font></tt>
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cite="mid:eb10968d-120c-9097-301c-de5469c78e52@ibcp.fr"><font
size="+1"><tt> Here is my procedure, please let me know what you
think: <br>
- convert .mrc map to .mtz ; I get F, PHIF.<br>
- supperpose the maps: <br>
map1: labels 2FOFCWT, PH2FOFCWT<br>
map2: F, PHIF.<br>
I also provided the 2 PDBs as it is clearly stated on the
input files definitions. <br>
<br>
It worked, with the 2 maps superposed that I can look and
compare. <br>
</tt></font></blockquote>
<br>
<tt><font size="+1">Ok, sounds good so far. Yes, this is what I
would expect!<br>
<br>
</font></tt>
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cite="mid:eb10968d-120c-9097-301c-de5469c78e52@ibcp.fr"><font
size="+1"><tt> However, for some reason, the superposition has
been done on chain C and D of the crystallograhic model
instead of chain AB (4 chains in the asymmetric unit, making 2
dimers). Is there a reason there, choosing the closest
structure, best fit? (I see that it is possible to define a
superposition) <br>
</tt></font></blockquote>
<br>
You can specify this manually!<br>
<br>
<blockquote type="cite"
cite="mid:eb10968d-120c-9097-301c-de5469c78e52@ibcp.fr"><font
size="+1"><tt> Another thing is that it creates a
"supperposition in the middle", meaning neither on model1 nor
model2 from the input, and not a crystallographic symmetric of
model1. So I can't use the full crystallographic maps, I have
a "simplified" version of it. <br>
</tt></font></blockquote>
<br>
<tt><font size="+1">I guess this is the feature of current
implementation.<br>
<br>
Pavel<br>
</font></tt><br>
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