3qac: Difference between revisions

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== Function ==

[https://www.uniprot.org/uniprot/Q38712_AMAHP Q38712_AMAHP]

== Publication Abstract from PubMed ==

11S globulin is one of the major seed storage proteins in amaranth. Recombinant protein was produced as up to approximately 80% of the total bacterial protein using Escherichia coli Rosetta-gami (DE3) containing pET21d with amaranth 11S globulin cDNA. The best expression condition was at 302 K for 20 h using LB medium containing 0.5 M NaCl. The recombinant protein was easily separated from most of the Escherichia coli proteins by precipitation with 0-40% ammonium sulfate solution. It formed aggregates at low temperature and at low salt concentrations. This behaviour may imply that it has a more hydrophobic nature than other 11S seed globulins. The crystals diffracted to 6 A resolution and belonged to space group P6(3), with unit-cell parameters a=b=97.6, c=74.8 A, gamma=120.0 degrees. One subunit of a trimer was estimated to be present in the asymmetric unit, assuming a Vsol of 41%. To obtain the complete structure solution, experiments to improve crystallization and flash-cooling conditions are in progress.

Expression, purification and preliminary crystallization of amaranth 11S proglobulin seed storage protein from Amaranthus hypochondriacus L.,Tandang-Silvas MR, Carrazco-Pena L, Barba de la Rosa AP, Osuna-Castro JA, Utsumi S, Mikami B, Maruyama N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt, 8):919-22. Epub 2010 Jul 29. PMID:020693668<ref>PMID:020693668</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 9: / Line 9: @@
 == Function ==
 [https://www.uniprot.org/uniprot/Q38712_AMAHP Q38712_AMAHP]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+S globulin is one of the major seed storage proteins in amaranth. Recombinant protein was produced as up to approximately 80% of the total bacterial protein using Escherichia coli Rosetta-gami (DE3) containing pET21d with amaranth 11S globulin cDNA. The best expression condition was at 302 K for 20 h using LB medium containing 0.5 M NaCl. The recombinant protein was easily separated from most of the Escherichia coli proteins by precipitation with 0-40% ammonium sulfate solution. It formed aggregates at low temperature and at low salt concentrations. This behaviour may imply that it has a more hydrophobic nature than other 11S seed globulins. The crystals diffracted to 6 A resolution and belonged to space group P6(3), with unit-cell parameters a=b=97.6, c=74.8 A, gamma=120.0 degrees. One subunit of a trimer was estimated to be present in the asymmetric unit, assuming a Vsol of 41%. To obtain the complete structure solution, experiments to improve crystallization and flash-cooling conditions are in progress.
+Expression, purification and preliminary crystallization of amaranth 11S proglobulin seed storage protein from Amaranthus hypochondriacus L.,Tandang-Silvas MR, Carrazco-Pena L, Barba de la Rosa AP, Osuna-Castro JA, Utsumi S, Mikami B, Maruyama N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt, 8):919-22. Epub 2010 Jul 29. PMID:020693668<ref>PMID:020693668</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3qac" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>