Number of the records: 1
Crystallization of nepenthesin I using a low-pH crystallization screen
- 1.0508211 - BTÚ 2020 RIV GB eng J - Journal Article
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
R&D Projects: GA MŠMT(CZ) ED1.1.00/02.0109
Institutional support: RVO:86652036
Keywords : aspartic protease nepenthesin-1 * isoelectric point * unique member
OECD category: Biochemistry and molecular biology
Impact factor: 0.799, year: 2016
Method of publishing: Limited access
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.
Permanent Link: http://hdl.handle.net/11104/0299182
Number of the records: 1