View source for 3wdn


==High-resolution X-ray crystal structure of bovine H-protein using a high-pressure cryocooling method==
<StructureSection load='3wdn' size='340' side='right'caption='[[3wdn]], [[Resolution|resolution]] 0.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wdn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WDN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.86&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdn OCA], [https://pdbe.org/3wdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wdn RCSB], [https://www.ebi.ac.uk/pdbsum/3wdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wdn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GCSH_BOVIN GCSH_BOVIN] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
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== Publication Abstract from PubMed ==
Recently, many technical improvements in macromolecular X-ray crystallography have increased the number of structures deposited in the Protein Data Bank and improved the resolution limit of protein structures. Almost all high-resolution structures have been determined using a synchrotron radiation source in conjunction with cryocooling techniques, which are required in order to minimize radiation damage. However, optimization of cryoprotectant conditions is a time-consuming and difficult step. To overcome this problem, the high-pressure cryocooling method was developed (Kim et al., 2005) and successfully applied to many protein-structure analyses. In this report, using the high-pressure cryocooling method, the X-ray crystal structure of bovine H-protein was determined at 0.86 A resolution. Structural comparisons between high- and ambient-pressure cryocooled crystals at ultra-high resolution illustrate the versatility of this technique. This is the first ultra-high-resolution X-ray structure obtained using the high-pressure cryocooling method.

High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method.,Higashiura A, Ohta K, Masaki M, Sato M, Inaka K, Tanaka H, Nakagawa A J Synchrotron Radiat. 2013 Nov;20(Pt 6):989-93. doi: 10.1107/S090904951302373X., Epub 2013 Oct 5. PMID:24121354<ref>PMID:24121354</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wdn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Higashiura A]]
[[Category: Nakagawa A]]