Cargando…
Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant
The crystallization of amidase, the ultimate enzyme in the Trp-dependent auxin-biosynthesis pathway, from Arabidopsis thaliana was attempted using protein samples with at least 95% purity. Cube-shaped crystals that were assumed to be amidase crystals that belonged to space group I4 (unit-cell parame...
Autores principales: | Andi, Babak, Soares, Alexei S., Shi, Wuxian, Fuchs, Martin R., McSweeney, Sean, Liu, Qun |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6718150/ https://www.ncbi.nlm.nih.gov/pubmed/31475929 http://dx.doi.org/10.1107/S2053230X19011488 |
Ejemplares similares
-
Discovery of Novel Dihydrolipoamide S-Succinyltransferase Inhibitors Based on Fragment Virtual Screening
por: Wei, Chengqian, et al.
Publicado: (2021) -
Multi-crystal native-SAD phasing at 5 keV with a helium environment
por: Karasawa, Akira, et al.
Publicado: (2022) -
Stabilization of Homoserine-O-Succinyltransferase (MetA) Decreases the Frequency of Persisters in Escherichia coli under Stressful Conditions
por: Mordukhova, Elena A., et al.
Publicado: (2014) -
Synchrotron microcrystal native-SAD phasing at a low energy
por: Guo, Gongrui, et al.
Publicado: (2019) -
Crystal Structure of Escherichia coli Agmatinase: Catalytic Mechanism and Residues Relevant for Substrate Specificity
por: Maturana, Pablo, et al.
Publicado: (2021)