Abstract
The cysteine protease inhibitor from Ascaris lumbricoides, a roundworm that lives in the human intestine, may be involved in the suppression of human immune responses. Here, the molecular cloning, protein expression and purification, preliminary crystallization and crystallographic characterization of the cysteine protease inhibitor from A. lumbricoides are reported. The rod-shaped crystal belonged to space group C2, with unit-cell parameters a = 99.40, b = 37.52, c = 62.92 Å, β = 118.26°. The crystal diffracted to 2.1 Å resolution and contained two molecules in the asymmetric unit.
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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Ascaris lumbricoides / enzymology*
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray / methods
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Cysteine Proteinase Inhibitors / chemistry*
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Cysteine Proteinase Inhibitors / genetics
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Cysteine Proteinase Inhibitors / isolation & purification
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Diffusion
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Escherichia coli / genetics
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Helminth Proteins / chemistry*
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High-Throughput Screening Assays
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Hot Temperature
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Humans
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Nematoda / parasitology
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Solubility
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Time Factors
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Transformation, Bacterial
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X-Ray Diffraction
Substances
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Cysteine Proteinase Inhibitors
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Helminth Proteins
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Recombinant Proteins