Literature DB >> 2113586

Crystallization and preliminary X-ray studies of the VL domain of the antibody McPC603 produced in Escherichia coli.

R Glockshuber1, B Steipe, R Huber, A Plückthun.   

Abstract

The VL domain, obtained from a recombinant Fv fragment of the antibody McPC603 expressed in Escherichia coli, has been crystallized as a dimer from 2 M-(NH4)2SO4 (pH 4.0). The crystals are hexagonal, space group P6(1)22. The cell dimensions are a = b = 86.48 A, c = 76.64 A, with a VL monomer as the asymmetric unit. The crystals diffract to 2.0 A. The structure was solved by Patterson search using the VL domain of the Fab fragment of McPC603 and the VL dimer REI.

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Year:  1990        PMID: 2113586     DOI: 10.1016/S0022-2836(05)80247-5

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Expression, purification and characterization of B72.3 Fv fragments.

Authors:  D J King; O D Byron; A Mountain; N Weir; A Harvey; A D Lawson; K A Proudfoot; D Baldock; S E Harding; G T Yarranton
Journal:  Biochem J       Date:  1993-03-15       Impact factor: 3.857

2.  Structure of a human monoclonal antibody Fab fragment against gp41 of human immunodeficiency virus type 1.

Authors:  X M He; F Rüker; E Casale; D C Carter
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-01       Impact factor: 11.205

  2 in total

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