Crystallization of nepenthesin I using a low-pH crystallization screen

0508211 - BTÚ 2020 RIV GB eng J - Článek v odborném periodiku
Fejfarová, Karla - Kádek, A. - Mrázek, H. - Hausner, J. - Tretyachenko, V. - Koval, T. - Man, P. - Hašek, Jindřich - Dohnálek, Jan
Crystallization of nepenthesin I using a low-pH crystallization screen.
Acta Crystallographica Section F-Structural Biology Communications. Roč. 72, JAN 2016 (2016), s. 24-28. E-ISSN 2053-230X
Grant CEP: GA MŠMT(CZ) ED1.1.00/02.0109
Institucionální podpora: RVO:86652036
Klíčová slova: aspartic protease nepenthesin-1 * isoelectric point * unique member
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 0.799, rok: 2016
Způsob publikování: Omezený přístup
http://scripts.iucr.org/cgi-bin/paper?S2053230X15022323

Nepenthesins are aspartic proteases secreted by carnivorous pitcher plants of the genus Nepenthes. They significantly differ in sequence from other plant aspartic proteases. This difference, which provides more cysteine residues in the structure of nepenthesins, may contribute to their unique stability profile. Recombinantly produced nepenthesin 1 ( rNep1) from N. gracilis in complex with pepstatin A was crystallized under two different crystallization conditions using a newly formulated low- pH crystallization screen.
Trvalý link: http://hdl.handle.net/11104/0299182