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Crystallization and Preliminary X-Ray Crystallographic Analysis of Human Serum Apotransferrin (CROSBI ID 517781)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa

Milić, Dalibor ; Bubaš, Valentina ; Matković-Čalogović, Dubravka Crystallization and Preliminary X-Ray Crystallographic Analysis of Human Serum Apotransferrin // Book of Abstracts. Fifteenth Slovenian-Croatian Crystallographic Meeting. 2006. str. 21-21-x

Podaci o odgovornosti

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

engleski

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

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.

human serum transferrin; protein crystallization; protein crystallography

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Podaci o prilogu

21-21-x.

2006.

objavljeno

Podaci o matičnoj publikaciji

Book of Abstracts. Fifteenth Slovenian-Croatian Crystallographic Meeting

Podaci o skupu

Fifteenth Slovenian-Croatian Crystallographic Meeting

predavanje

01.01.2006-01.01.2006

Jezersko, Slovenija

Povezanost rada

Kemija