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Conformational Change of the Adenovirus DNA-Binding Protein Induced by Soaking Crystals with K3UO2F5 Solutions (1996)

Kanellopoulos, P. N. ; Tsernoglou, D. ; van der Vliet, P. C. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 52 (1996), S. 942-945

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: Soaking crystals of the C-terminal DNA-binding domain of the adenovirus single-stranded DNA-binding protein with a buffer containing K3UO2F5 results in a 9% change of the crystallographic c axis without destruction of the crystals or appreciable loss of resolution. The crystals belong to space group P212121 with a = 79.7, b = 75.6 and c = 60.6 Å. The three-dimensional structure has been refined to 2.7 Å with a crystallographic R factor of 0.206. Antiparallel chains of protein molecules running through the entire crystal are linked by uranyl ions. The relative orientation of protein monomers is flexible, even in the crystalline state, and allows changes in the packing of the protein chains.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444996005525

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