2021
DOI: 10.1039/d1nr00268f
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LEAFY protein crystals with a honeycomb structure as a platform for selective preparation of outstanding stable bio-hybrid materials

Abstract: Well-organized protein assemblies offer many properties that justify their use for the design of innovative bionanomaterials. Here, crystals of the oligomerization domain of the LEAFY protein from Ginkgo biloba, organized...

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Cited by 2 publications
(10 citation statements)
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“…These residues remain invisible by X-ray crystallography (Fig. 1) because of their flexible structure, but their presence was confirmed by mass spectrometry 35 . GbLFY-SAM proteins were expressed in Escherichia coli BL21(DE3) strain.…”
Section: Protein Synthesis and Purificationmentioning
confidence: 89%
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“…These residues remain invisible by X-ray crystallography (Fig. 1) because of their flexible structure, but their presence was confirmed by mass spectrometry 35 . GbLFY-SAM proteins were expressed in Escherichia coli BL21(DE3) strain.…”
Section: Protein Synthesis and Purificationmentioning
confidence: 89%
“…These residues remain invisible in the X-ray crystallography images (Figure 1) because of their flexible structure, but their presence was confirmed by mass spectrometry. 35 GbLFY-SAM proteins were expressed in Escherichia coli BL21(DE3) strain. First, cells were transformed with pETM11 plasmid coding for an Nterminal histidine tag and a tobacco etch virus protease cleavage site for the N-terminal extension (referred as TEV) followed by the sequence corresponding to GbLFY-SAM wild type protein.…”
Section: Methodsmentioning
confidence: 99%
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