Crystallization of a soluble form of the rat T-cell surface glycoprotein CD4 complexed with Fab from the W3/25 monoclonal antibody

Simon J. Davis; R. Leo Brady; A. Neil Barclay; Karl Harlos; G. Guy Dodson; Alan F. Williams

doi:10.1016/S0022-2836(05)80116-0

Crystallization of a soluble form of the rat T-cell surface glycoprotein CD4 complexed with Fab from the W3/25 monoclonal antibody

Simon J. Davis^*, R. Leo Brady, A. Neil Barclay, Karl Harlos, G. Guy Dodson, Alan F. Williams

^*Corresponding author for this work

Research output: Contribution to journal › Article (Academic Journal) › peer-review

23 Citations (Scopus)

Abstract

The structure of the T-lymphocyte cell surface glycoprotein CD4 is of considerable biological and medical interest. Recombinant rat CD4 expressed in soluble form in mammalian cells and complexed with W3/25 monoclonal Fab fragments formed crystals that diffract to 3·5 Å and have the orthorhombic space group P2₁2₁2 or P2₁2₁2₁. The unit cell has dimensions a = 317 Å, b = 161 Å and c = 41·8 Å and the asymmetric unit consists of two CD4 : Fab complexes. These crystals are of suitable quality for X-ray diffraction analysis.

Original language	English
Pages (from-to)	7-10
Number of pages	4
Journal	Journal of Molecular Biology
Volume	213
Issue number	1
DOIs	https://doi.org/10.1016/S0022-2836(05)80116-0
Publication status	Published - 5 May 1990

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title = "Crystallization of a soluble form of the rat T-cell surface glycoprotein CD4 complexed with Fab from the W3/25 monoclonal antibody",

abstract = "The structure of the T-lymphocyte cell surface glycoprotein CD4 is of considerable biological and medical interest. Recombinant rat CD4 expressed in soluble form in mammalian cells and complexed with W3/25 monoclonal Fab fragments formed crystals that diffract to 3·5 {\AA} and have the orthorhombic space group P21212 or P212121. The unit cell has dimensions a = 317 {\AA}, b = 161 {\AA} and c = 41·8 {\AA} and the asymmetric unit consists of two CD4 : Fab complexes. These crystals are of suitable quality for X-ray diffraction analysis.",

author = "Davis, {Simon J.} and Brady, {R. Leo} and Barclay, {A. Neil} and Karl Harlos and Dodson, {G. Guy} and Williams, {Alan F.}",

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T1 - Crystallization of a soluble form of the rat T-cell surface glycoprotein CD4 complexed with Fab from the W3/25 monoclonal antibody

AU - Davis, Simon J.

AU - Brady, R. Leo

AU - Barclay, A. Neil

AU - Harlos, Karl

AU - Dodson, G. Guy

AU - Williams, Alan F.

PY - 1990/5/5

Y1 - 1990/5/5

N2 - The structure of the T-lymphocyte cell surface glycoprotein CD4 is of considerable biological and medical interest. Recombinant rat CD4 expressed in soluble form in mammalian cells and complexed with W3/25 monoclonal Fab fragments formed crystals that diffract to 3·5 Å and have the orthorhombic space group P21212 or P212121. The unit cell has dimensions a = 317 Å, b = 161 Å and c = 41·8 Å and the asymmetric unit consists of two CD4 : Fab complexes. These crystals are of suitable quality for X-ray diffraction analysis.

AB - The structure of the T-lymphocyte cell surface glycoprotein CD4 is of considerable biological and medical interest. Recombinant rat CD4 expressed in soluble form in mammalian cells and complexed with W3/25 monoclonal Fab fragments formed crystals that diffract to 3·5 Å and have the orthorhombic space group P21212 or P212121. The unit cell has dimensions a = 317 Å, b = 161 Å and c = 41·8 Å and the asymmetric unit consists of two CD4 : Fab complexes. These crystals are of suitable quality for X-ray diffraction analysis.

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

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ER -

Crystallization of a soluble form of the rat T-cell surface glycoprotein CD4 complexed with Fab from the W3/25 monoclonal antibody

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