Journal:Acta Cryst F:S1744309112003326

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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The use of whole insect larvae as a source of recombinant proteins offers a more cost-effective method of producing large quantities of human proteins than conventional cell-culture approaches. Human carboxylesterase 1 has been produced in and isolated from whole ''Trichoplusia ni'' larvae. The recombinant protein was crystallized and its structure was solved to 2.2 Å resolution. The results indicate that the larvae-produced enzyme is essentially identical to that isolated from cultured Sf21 cells, supporting the use of this expression system to produce recombinant enzymes for crystallization studies.
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The use of whole insect larvae as a source of recombinant proteins offers a more cost-effective method of producing large quantities of human proteins than conventional cell-culture approaches. Human carboxylesterase 1 (rhCES1) has been produced in and isolated from whole ''Trichoplusia ni'' larvae. The recombinant protein was crystallized and its structure was solved to 2.2 Å resolution. The results indicate that the larvae-produced enzyme is essentially identical to that isolated from cultured Sf21 cells, supporting the use of this expression system to produce recombinant enzymes for crystallization studies.
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The current structure of rhCES1 represents the first published hexagonal crystal form, despite the fact that all other published examples of hCES1 structures consist of a hexamer in the asymmetric unit. The trimer of subunits sits around one of the threefold axes found in this space group, while the three twofold axes at z = 1/4 that intersect on this axis complete the hexamer.
</StructureSection>
</StructureSection>

Revision as of 13:55, 7 February 2012

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