5i18 | pdb_00005i18
From Proteopedia
CRYSTAL STRUCTURE OF HUMAN GERMLINE ANTIBODY IGHV1-69/IGKV4-1
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Structural highlights
Publication Abstract from PubMedThe crystallization of 16 human antibody Fab fragments constructed from all pairs of four different heavy chains and four different light chains was enabled by employing microseed matrix screening (MMS). In initial screening, diffraction-quality crystals were obtained for only three Fabs, while many Fabs produced hits that required optimization. Application of MMS, using the initial screens and/or refinement screens, resulted in diffraction-quality crystals of these Fabs. Five Fabs that failed to give hits in the initial screen were crystallized by cross-seeding MMS followed by MMS optimization. The crystallization protocols and strategies that resulted in structure determination of all 16 Fabs are presented. These results illustrate the power of MMS and provide a basis for developing future strategies for macromolecular crystallization. Protein crystallization with microseed matrix screening: application to human germline antibody Fabs.,Obmolova G, Malia TJ, Teplyakov A, Sweet RW, Gilliland GL Acta Crystallogr F Struct Biol Commun. 2014 Aug;70(Pt 8):1107-15. doi:, 10.1107/S2053230X14012552. Epub 2014 Jul 23. PMID:25084393[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 18:02, 26 February 2016.