著者

有森 貴夫

出版者

日本結晶学会

雑誌

日本結晶学会誌 (ISSN:03694585)

巻号頁・発行日

vol.63, no.2, pp.113-120, 2021-05-31 (Released:2021-06-05)

参考文献数

26

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In the protein crystallography, antibodies are frequently used as ‘crystallization chaperones’, where their binding facilitates production of high-quality diffracting crystals of complex macromolecules that are otherwise resistant to crystallization. To develop an ideal antibody fragment, we have designed a novel antibody fragment format, called ‘Fv-clasp’, that is a fusion of an anti-parallel coiled-coil structure derived from the hMst1 SARAH domain to the Fv fragment of an antibody. We have demonstrated that Fv-clasp has superior properties over conventional antibody fragments including Fab and single-chain Fv(scFv)in terms of producibility, stability, and crystallizability.