Title : Structure of Recombinant Human Carboxylesterase 1 Isolated from Whole Cabbage Looper Larvae - Greenblatt_2012_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_F68_269 |
Author(s) : Greenblatt HM , Otto TC , Kirkpatrick MG , Kovaleva E , Brown S , Buchman G , Cerasoli DM , Sussman JL |
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , F68 :269 , 2012 |
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. |
PubMedSearch : Greenblatt_2012_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_F68_269 |
PubMedID: 22442219 |
Gene_locus related to this paper: human-CES1 |
Gene_locus | human-CES1 |
Structure | 4AB1 |
Greenblatt HM, Otto TC, Kirkpatrick MG, Kovaleva E, Brown S, Buchman G, Cerasoli DM, Sussman JL (2012)
Structure of Recombinant Human Carboxylesterase 1 Isolated from Whole Cabbage Looper Larvae
Acta Crystallographica Sect F Struct Biol Cryst Commun
F68 :269
Greenblatt HM, Otto TC, Kirkpatrick MG, Kovaleva E, Brown S, Buchman G, Cerasoli DM, Sussman JL (2012)
Acta Crystallographica Sect F Struct Biol Cryst Commun
F68 :269