Crystallization of nepenthesin I using a low-pH crystallization screen

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00457610" target="_blank" >RIV/61388971:_____/16:00457610 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61389013:_____/16:00457610 RIV/00216208:11310/16:10324222 RIV/86652036:_____/16:00508211

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S2053230X15022323" target="_blank" >http://dx.doi.org/10.1107/S2053230X15022323</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2053230X15022323" target="_blank" >10.1107/S2053230X15022323</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Crystallization of nepenthesin I using a low-pH crystallization screen

Popis výsledku v původním jazyce

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, [alpha] = [beta] = [gamma] = 90° and a = 86.28, b = 97.22, c = 103.78 Å, [alpha] = [beta] = [gamma] = 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.

Název v anglickém jazyce

Crystallization of nepenthesin I using a low-pH crystallization screen

Popis výsledku anglicky

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, [alpha] = [beta] = [gamma] = 90° and a = 86.28, b = 97.22, c = 103.78 Å, [alpha] = [beta] = [gamma] = 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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS

ISSN

2053-230X

e-ISSN

—

Svazek periodika

72

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

5

Strana od-do

24-28

Kód UT WoS článku

000369379700005

EID výsledku v databázi Scopus

2-s2.0-84954317484