| Literature DB >> 22442219 |
Harry M Greenblatt1, Tamara C Otto, Melanie G Kirkpatrick, Elena Kovaleva, Susan Brown, George Buchman, Douglas M Cerasoli, Joel L Sussman.
Abstract
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 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.Entities:
Mesh:
Substances:
Year: 2012 PMID: 22442219 PMCID: PMC3310527 DOI: 10.1107/S1744309112003326
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091