Purification, crystallization and preliminary crystallographic study of a recombinant plant aminoaldehyde dehydrogenase from Pisum sativum
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18259056
PubMed Central
PMC2374172
DOI
10.1107/s1744309107068522
PII: S1744309107068522
Knihovny.cz E-zdroje
- MeSH
- aldehyddehydrogenasa chemie izolace a purifikace metabolismus MeSH
- DNA primery MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- hrách setý enzymologie MeSH
- klonování DNA MeSH
- konformace proteinů MeSH
- krystalizace MeSH
- krystalografie rentgenová MeSH
- rekombinantní proteiny chemie izolace a purifikace metabolismus MeSH
- sekvence nukleotidů MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
- western blotting MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aldehyddehydrogenasa MeSH
- DNA primery MeSH
- rekombinantní proteiny MeSH
Aminoaldehydes are products of polyamine degradation and are known to be reactive metabolites that are toxic to living cells at high concentrations. These compounds are catabolized by aminoaldehyde dehydrogenases, which are enzymes that contain a nicotinamide adenine dinucleotide coenzyme. Aminoaldehyde dehydrogenase from Pisum sativum was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop method. A complete data set was collected to 2.8 A resolution at 100 K. Crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 86.4, b = 216.6, c = 205.4 A, beta = 98.1 degrees. Molecular replacement was performed and led to the identification of six dimers per asymmetric unit.
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