Journal:Acta Cryst F:S1744309112003326
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='HH.pdb' size='500' side='right' scene='Journal:Acta_Cryst_F:1/Cv/ | + | <StructureSection load='HH.pdb' size='500' side='right' scene='Journal:Acta_Cryst_F:1/Cv/2' caption=''> |
=== Title Of The Paper === | === Title Of The Paper === | ||
<big>Harry M. Greenblatt, Tamara C. Otto, Melanie G. Kirkpatrick, Elena Kovaleva, Susan Brown,George Buchman, Douglas M. Cerasoli and Joel L. Sussman</big><ref >no ref yet</ref> | <big>Harry M. Greenblatt, Tamara C. Otto, Melanie G. Kirkpatrick, Elena Kovaleva, Susan Brown,George Buchman, Douglas M. Cerasoli and Joel L. Sussman</big><ref >no ref yet</ref> | ||
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | + | 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. | |
</StructureSection> | </StructureSection> | ||
Revision as of 13:53, 7 February 2012
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