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• W2018575563 abstract "The three-dimensional structure of ceruloplasmin (CP) with unoccupied labile metal-binding sites and the structure of CP containing Ni2+ in the labile sites were solved for the first time at 2.6 and 2.95 Å resolution, respectively. Crystallization was performed with the use of storage-stable CP, which was prepared in the presence of proteinase inhibitors and purified from (pre)proteinases. Ceruloplasmin with Ni2+ crystallized in the orthorhombic space group, which had been earlier unknown for CP. Ceruloplasmin with the unoccupied labile sites crystallized in the trigonal crystal form. The differences in intermolecular contacts observed in the trigonal and orthorhombic crystal structures of CP are considered. The conformational changes attendant upon Ni2+ binding are described. It was suggested that the labile sites are multifunctional and can both bind metal ions potentially toxic to organisms and be involved in electron transfer from substrates to the active site." @default.
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• W2018575563 date "2008-07-01" @default.
• W2018575563 modified "2023-10-10" @default.
• W2018575563 title "X-ray diffraction study of highly purified human ceruloplasmin" @default.
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• W2018575563 doi "https://doi.org/10.1134/s1063774508040172" @default.
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