Preliminary X-ray analysis of a human VH fragment at 1.8 Å resolution

Authors: Gaur, Rajneesh Kumar; Kupper, Michael B.; Fischer, Rainer; Hoffmann, Kurt M. V.

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 965-967(3)

Publisher: Blackwell Publishing

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Abstract:

Small antibody fragments are more useful than full-size antibodies for achieving efficient biodistribution. As a first step towards the design of a clinically desirable antibody fragment, the crystallization of a human VH fragment has been achieved. The fragment was derived from the single-chain antibody scFvM12, which recognizes a cancer-specific hypoglycosylated form of mucin. The VH fragment was obtained by in-drop digestion of the scFvM12 with a low concentration of the broad-spectrum protease subtilisin Carlsberg. The crystal belongs to the monoclinic space group C2. The crystal diffracted to 1.8 Å resolution when analysed at 100 K using a rotating-anode X-ray generator.

Keywords: MUC1; cancer marker; VH fragment; ESI-MS/MS; proteases

Document Type: Research article

DOI: 10.1107/S0907444904004834

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