Naslov
Crystallization and Preliminary X-Ray Crystallographic Analysis of Human Serum Apotransferrin

Autori
Milić, Dalibor ; Bubaš, Valentina ; Matković-Čalogović, Dubravka

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of Abstracts. Fifteenth Slovenian-Croatian Crystallographic Meeting / - , 2006, 21-21

Skup
Fifteenth Slovenian-Croatian Crystallographic Meeting

Mjesto i datum
Jezersko, Slovenija, 15.06.2006. - 18.06.2006

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
human serum transferrin; protein crystallization; protein crystallography

Sažetak
The serum transferrins are vertebrate bilobal glycoproteins that bind ferric ions in the bloodstream and transport them to cells [E. N. Baker, Adv. Inorg. Chem. 41 (1994) 389]. The crystal structures of diferric serum transferrins from hen [P. G. Thakurta, et al., D. Choudhury, R. Dasgupta, J. K. Dattagupta, Acta Crystallogr. Sect. D 59 (2003) 1773], pig and rabbit [D. R. Hall, et al., Acta Crystallogr. Sect. D 58 (2002) 70] were determined so far. Each transferrin molecule consists of two homologous lobes (N- and C-lobes). The lobes are further divided into two dissimilar domains with the iron binding site positioned in the interdomain cleft of each lobe. Several crystal structures of the recombinant N-terminal half-molecule of human serum transferrin holo and apo forms are also known [R. T. A. McGillivray, et al., Biochemistry 37 (1998) 7919 ; D. Jeffrey, et al., Biochemistry 37 (1998) 13978], while the structure of the whole human serum transferrin molecule with both lobes in the apo (iron-free) form is still unknown. Crystals of human serum apotransferrin were grown using the sitting-drop vapor-diffusion method and polyethylene glycol 3350 as a precipitating agent. The crystals belong to space group P212121, with unit cell parameters a = 84.49 Ǻ , b = 99.87 Ǻ , c = 197.71 Ǻ , and have two apotransferrin molecules in the asymmetric unit. Data sets were collected to 3.9 Ǻ on cryocooled crystals (200 K) at the ELETTRA Synchrotron Light Source (Trieste). Further optimization of the crystallization conditions in order to obtain better diffracting crystals is in progress.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA