Publication: Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus
Issued Date
2007-04-28
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ISSN
17443091
17443091
17443091
Other identifier(s)
2-s2.0-34248138356
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Mahidol University
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SCOPUS
Bibliographic Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.63, No.5 (2007), 386-392
Suggested Citation
Pojchong Chotiyarnwong, Guillaume B. Stewart-Jones, Michael J. Tarry, Wanwisa Dejnirattisai, Christian Siebold, Michael Koch, David I. Stuart, Karl Harlos, Prida Malasit, Gavin Screaton, Juthathip Mongkolsapaya, E. Yvonne Jones Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.63, No.5 (2007), 386-392. doi:10.1107/S1744309107013693 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/24208
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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
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.