Title : Crystallization and preliminary X-ray study of a recombinant cutinase from Fusarium solani pisi - Abergel_1990_J.Mol.Biol_215_215 |
Author(s) : Abergel C , Martinez C , Fontecilla-Camps JC , Cambillau C , de Geus P , Lauwereys M |
Ref : Journal of Molecular Biology , 215 :215 , 1990 |
Abstract :
Recombinant cutinase from Fusarium solani pisi is expressed and excreted with very high yields in Escherichia coli cultures. Cutinase was crystallized at 20 degrees C using the vapour diffusion technique, with polyethylene glycol 6000 as precipitant. Best crystals were obtained at pH 7.0 with polyethylene glycol 6000 as precipitant. Best crystals were obtained at pH 7.0 with polyethylene glycol at 15 to 20%. They are monoclinic, with space group P2(1) and cell dimensions a = 35.1 A, b = 67.4 A, c = 37.05 A and beta = 94.0 degrees; they diffract beyond 1.5 A resolution. The asymmetric unit contains one molecule of 22,000 Da (Vm = 1.98 A3/Da; 38% water). |
PubMedSearch : Abergel_1990_J.Mol.Biol_215_215 |
PubMedID: 2213880 |
Abergel C, Martinez C, Fontecilla-Camps JC, Cambillau C, de Geus P, Lauwereys M (1990)
Crystallization and preliminary X-ray study of a recombinant cutinase from Fusarium solani pisi
Journal of Molecular Biology
215 :215
Abergel C, Martinez C, Fontecilla-Camps JC, Cambillau C, de Geus P, Lauwereys M (1990)
Journal of Molecular Biology
215 :215