Abstract
We have cloned and expressed in Escherichia coli cDNA for rat nuclear transport factor 2 (NTF2), a key cytoplasmic factor that facilitates the import of proteins into the nucleus through nuclear pores. We have used this bacterially expressed material to produce orthorhombic crystals suitable for high-resolution X-ray diffraction structure determination. The crystals have P212121 symmetry with a = 55.9 A; b = 56.7 A; c = 88.3 A and diffract past 2 A on laboratory X-ray sources. The asymmetric unit of these crystals contains two NTF2 polypeptide chains, consistent with the reported dimeric structure of the molecule.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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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, Complementary / genetics
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / isolation & purification
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Nucleocytoplasmic Transport Proteins*
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Protein Conformation
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Rats
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / isolation & purification
Substances
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Carrier Proteins
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DNA, Complementary
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Nuclear Proteins
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Nucleocytoplasmic Transport Proteins
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Nutf2 protein, rat
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Recombinant Fusion Proteins