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Engineering of recombinant crystallization chaperones
- Source :
- Current Opinion in Structural Biology. 19:449-457
- Publication Year :
- 2009
- Publisher :
- Elsevier BV, 2009.
-
Abstract
- The preparation of diffraction quality crystals remains the major bottleneck in macromolecular X-ray crystallography. A crystallization chaperone is an auxiliary protein, such as fragments of monoclonal antibodies, that binds to and increases the crystallization probability of a target molecule of interest. Such chaperones reduce conformational heterogeneity, mask counterproductive surfaces while extending surfaces predisposed to forming crystal contacts, and provide phasing information. Crystallization chaperones generated using recombinant technologies have emerged as superior alternatives that increase the throughput and eliminate inherent limitations associated with antibody production by animal immunization and the hybridoma technology.
- Subjects :
- medicine.drug_class
Protein Engineering
Monoclonal antibody
Article
Antibodies
Protein Structure, Secondary
law.invention
Structural Biology
law
medicine
Animals
Humans
Crystallization
Molecular Biology
biology
Chemistry
Recombinant Proteins
Antibody production
Biochemistry
Chaperone (protein)
Recombinant DNA
Biophysics
biology.protein
Hybridoma technology
Chemical chaperone
Molecular Chaperones
Macromolecule
Subjects
Details
- ISSN :
- 0959440X
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Current Opinion in Structural Biology
- Accession number :
- edsair.doi.dedup.....db1ced4a8fb4ab1d7fed7fa793837960
- Full Text :
- https://doi.org/10.1016/j.sbi.2009.04.008