Crystallization of nepenthesin I using a low-pH crystallization screen
Result description
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.
Keywords
aspartic protease nepenthesin-1isoelectric pointunique member
The result's identifiers
Result code in IS VaVaI
Alternative codes found
RIV/61388971:_____/16:00457610 RIV/61389013:_____/16:00457610 RIV/00216208:11310/16:10324222
Result on the web
DOI - Digital Object Identifier
Alternative languages
Result language
angličtina
Original language name
Crystallization of nepenthesin I using a low-pH crystallization screen
Original language description
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.
Czech name
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Czech description
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Classification
Type
Jimp - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section F - Structural Biology Communications
ISSN
2053-230X
e-ISSN
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Volume of the periodical
72
Issue of the periodical within the volume
JAN 2016
Country of publishing house
GB - UNITED KINGDOM
Number of pages
5
Pages from-to
24-28
UT code for WoS article
000369379700005
EID of the result in the Scopus database
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Basic information
Result type
Jimp - Article in a specialist periodical, which is included in the Web of Science database
OECD FORD
Biochemistry and molecular biology
Year of implementation
2016