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Crystallization of nepenthesin I using a low-pH crystallization screen

K. Fejfarová, A. Kádek, H. Mrázek, J. Hausner, V. Tretyachenko, T. Koval', P. Man, J. Hašek, J. Dohnálek,

. 2016 ; 72 (Pt 1) : 24-8. [pub] 20160101

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc17000668
E-zdroje Online Plný text

NLK Free Medical Journals od 2014 do Před 2 roky
PubMed Central od 2014 do Před 1 rokem
Europe PubMed Central od 2014 do Před 2 roky

Odkazy

PubMed 26750480
DOI 10.1107/s2053230x15022323
Knihovny.cz E-zdroje

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. The diffraction data were processed to 2.9 and 2.8 Å resolution, respectively. The crystals belonged to space group P212121, with unit-cell parameters a = 86.63, b = 95.90, c = 105.40 Å, α = β = γ = 90° and a = 86.28, b = 97.22, c = 103.78 Å, α = β = γ = 90°, respectively. Matthews coefficient and solvent-content calculations suggest the presence of two molecules of rNep1 in the asymmetric unit. Here, the details of the crystallization experiment and analysis of the X-ray data are reported.

Citace poskytuje Crossref.org

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