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Crystallization and preliminary crystallographic studies of a cysteine protease inhibitor from the human nematode parasite Ascaris lumbricoides
- Publication Year :
- 2011
- Publisher :
- International Union of Crystallography, 2011.
-
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 A, β = 118.26°. The crystal diffracted to 2.1 A resolution and contained two molecules in the asymmetric unit.
- Subjects :
- Hot Temperature
Time Factors
Human intestine
Nematoda
Biophysics
Molecular cloning
Biology
Cysteine Proteinase Inhibitors
Crystallography, X-Ray
Biochemistry
Protein expression
law.invention
Diffusion
Immune system
X-Ray Diffraction
Structural Biology
law
Genetics
Escherichia coli
Animals
Humans
Amino Acid Sequence
Crystallization
Cloning, Molecular
Ascaris lumbricoides
Sequence Homology, Amino Acid
Helminth Proteins
Condensed Matter Physics
biology.organism_classification
Molecular biology
Cysteine protease
Recombinant Proteins
Nematode parasite
High-Throughput Screening Assays
Crystallography
Solubility
Crystallization Communications
Transformation, Bacterial
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....3d2c964a52142a64f30c9e86ac8385cf