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Journal Article

Five viral peptide-HLA-A2 co-crystals. Simultaneous space group determination and X-ray data collection


Madden,  Dean R.
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

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Garboczi, D. N., Madden, D. R., & Wiley, D. C. (1994). Five viral peptide-HLA-A2 co-crystals. Simultaneous space group determination and X-ray data collection. Journal of Molecular Biology (London), 239(4), 581-587. doi:doi:10.1006/jmbi.1994.1398.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-A906-7
We prepared and crystallized five complexes of the human histocompatibility molecule HLA-A2 with peptides derived from human immunodeficiency virus type 1, human T lymphotropic virus type 1, influenza A virus and hepatitis B virus proteins. Each HLA-A2 complex was refolded in vitro from insoluble proteins produced in bacteria; to crystallize, two of the complexes required seeding with microcrystals of another complex. Maintained at -160 degrees C, single co-crystals of each of the five peptide-HLA-A2 complexes yielded complete X-ray diffraction data sets to a resolution of approximately 2.5 A. After a sufficient number of diffraction peaks were acquired during data collection, the direct analysis of integrated intensities established the point group of the co-crystal, thus allowing an efficient data collection strategy to be designed. The subsequent examination of systematic absences revealed that the five peptide-HLA-A2 co-crystals formed in space groups P1, P2(1), or P2(1)2(1)2(1). Molecular replacement structure solutions yielded unambiguous protein electron density maps, thus confirming the space group determinations. The system of obtaining HLA-A2 co-crystal structures described here is applicable to other crystallographic problems where structures of several related molecules from uncharacterized single crystals are required.