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|Title:||Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus|
Guillaume B. Stewart-Jones
Michael J. Tarry
David I. Stuart
E. Yvonne Jones
Division of Structural Biology and Oxford Protein Production Facility
Thailand National Center for Genetic Engineering and Biotechnology
University of Oxford
|Keywords:||Biochemistry, Genetics and Molecular Biology;Physics and Astronomy|
|Citation:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.63, No.5 (2007), 386-392|
|Abstract:||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. © International Union of Crystallography 2007.|
|Appears in Collections:||Scopus 2006-2010|
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