<html><head></head><body style="word-wrap: break-word; -webkit-nbsp-mode: space; -webkit-line-break: after-white-space; ">really fascinating, bringing back the discussion for a repository for your collected frames.<div><br></div><div>Jürgen</div><div><br><div><br></div><div><span class="Apple-style-span" style="font-family: Times; "><i>Acta Cryst.</i></span><span class="Apple-style-span" style="font-family: Times; "> </span><span class="Apple-style-span" style="font-family: Times; ">(2012). F</span><span class="Apple-style-span" style="font-family: Times; "><b>68</b></span><span class="Apple-style-span" style="font-family: Times; ">, 366-376 </span></div><div><a href="http://dx.doi.org/10.1107/S1744309112008421">doi:10.1107/S1744309112008421</a><div><font class="Apple-style-span" face="Times"><i><br></i></font></div><div><font class="Apple-style-span" face="Times"><h3 style="margin-top: 0em; margin-bottom: 0.5em; padding-top: 0em; padding-right: 0em; padding-bottom: 0em; padding-left: 0em; ">Detection and analysis of unusual features in the structural model and structure-factor data of a birch pollen allergen</h3><h3 style="margin-top: 0em; margin-bottom: 0.5em; padding-top: 0em; padding-right: 0em; padding-bottom: 0em; padding-left: 0em; "><a href="http://scripts.iucr.org/cgi-bin/citedin?search_on=name&author_name=Rupp,%20B." style="color: rgb(0, 0, 102); text-decoration: none; ">B. Rupp</a></h3><p><b>Abstract:</b> Physically improbable features in the model of the birch pollen structure Bet v 1d (PDB entry <a href="http://pdb.pdb.bnl.gov/pdb-bin/opdbshort?3k78" style="color: rgb(0, 0, 102); text-decoration: none; ">3k78</a>) are faithfully reproduced in electron density generated with the deposited structure factors, but these structure factors themselves exhibit properties that are characteristic of data calculated from a simple model and are inconsistent with the data and error model obtained through experimental measurements. The refinement of the <a href="http://pdb.pdb.bnl.gov/pdb-bin/opdbshort?3k78" style="color: rgb(0, 0, 102); text-decoration: none; ">3k78</a>model against these structure factors leads to an isomorphous structure different from the deposited model with an implausibly small <span class="it"><i>R</i></span> value (0.019). The abnormal refinement is compared with normal refinement of an isomorphous variant structure of Bet v 1l (PDB entry <a href="http://pdb.pdb.bnl.gov/pdb-bin/opdbshort?1fm4" style="color: rgb(0, 0, 102); text-decoration: none; ">1fm4</a>). A variety of analytical tools, including the application of Diederichs plots, <span class="it"><i>R</i></span><img alt="[sigma]" border="0" id="7adfdc79-e058-41f1-a172-5de653b0a333" height="7" width="8" apple-width="yes" apple-height="yes" src="cid:4DF2E3F0-3FD2-4B6A-BA27-9E22B8A07F37@hsd1.md.comcast.net."> plots and bulk-solvent analysis are discussed as promising aids in validation. The examination of the Bet v 1d structure also cautions against the practice of indicating poorly defined protein chain residues through zero occupancies. The recommendation to preserve diffraction images is amplified.</p></font><div apple-content-edited="true">
......................<br>Jürgen Bosch<br>Johns Hopkins University<br>Bloomberg School of Public Health<br>Department of Biochemistry & Molecular Biology<br>Johns Hopkins Malaria Research Institute<br>615 North Wolfe Street, W8708<br>Baltimore, MD 21205<br>Office: +1-410-614-4742<br>Lab: +1-410-614-4894<br>Fax: +1-410-955-2926<br><a href="http://web.mac.com/bosch_lab/">http://web.mac.com/bosch_lab/</a><br><br><br><br>
</div>
<br></div></div></div></body></html>