Expression, purification, cocrystallization and preliminary crystallographic analysis of sucrose octasulfate/human complement regulator factor H SCRs 6-8

Beverly E. Prosser, Steven Johnson, Pietro Roversi, Simon J. Clark, Edward Tarelli, Robert B. Sim, Antony J. Day, Susan M. Lea

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Human plasma protein complement factor H (FH) is an inhibitor of the spontaneously activated alternative complement pathway. An allotypic variant of FH, 402His, has been associated with age-related macular degeneration, the leading cause of blindness in the elderly. Crystals of FH domains 6-8 (FH678) containing 402His have been grown in the presence of a polyanionic sucrose octasulfate ligand (an analogue of the natural glycosaminoglycan ligands of FH) using both native and selenomethionine-derivatized protein. Native data sets diffracting to 2.3 Å and SeMet data sets of up to 2.8 Å resolution have been collected. An anomalous difference Patterson map reveals self- and cross-peaks from two incorporated Se atoms. The corresponding selenium substructure has been solved. © International Union of Crystallography 2007.
    Original languageEnglish
    Pages (from-to)480-483
    Number of pages3
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume63
    Issue number6
    DOIs
    Publication statusPublished - 5 May 2007

    Keywords

    • Age-related macular degeneration
    • Complement factor H
    • Complement regulator
    • Short consensus repeat
    • Sucrose octasulfate

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