Abstract
The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02 Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / isolation & purification*
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Crystallization
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Crystallography, X-Ray
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DNA Helicases
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Humans
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Molecular Sequence Data
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Poly-ADP-Ribose Binding Proteins
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Protein Conformation*
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Protein Isoforms / chemistry*
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Protein Isoforms / genetics
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Protein Isoforms / isolation & purification*
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RNA Helicases
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RNA Recognition Motif Proteins
Substances
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Carrier Proteins
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Poly-ADP-Ribose Binding Proteins
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Protein Isoforms
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RNA Recognition Motif Proteins
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DNA Helicases
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G3BP1 protein, human
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RNA Helicases