Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus
- Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London (United Kingdom)
- Division of Structural Biology and Oxford Protein Production Facility (OPPF), The Henry Wellcome Building for Genomic Medicine, Roosevelt Drive, Headington, Oxford OX3 7BN (United Kingdom)
- Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University (Thailand)
Crystals of an MHC class I molecule bound to naturally occurring peptide variants from the dengue virus NS3 protein contained high levels of solvent and required optimization of cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process facilitated by the use of a free-mounting system. T-cell recognition of the antigenic peptides presented by MHC class I molecules normally triggers protective immune responses, but can result in immune enhancement of disease. Cross-reactive T-cell responses may underlie immunopathology in dengue haemorrhagic fever. To analyze these effects at the molecular level, the functional MHC class I molecule HLA-A*1101 was crystallized bound to six naturally occurring peptide variants from the dengue virus NS3 protein. The crystals contained high levels of solvent and required optimization of the cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process that was facilitated by the use of a free-mounting system.
- OSTI ID:
- 22360322
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 5; Other Information: PMCID: PMC2334998; PMID: 17565177; PUBLISHER-ID: en5229; OAI: oai:pubmedcentral.nih.gov:2334998; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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