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Crystals of an antibody F V fragment against an integral membrane protein diffracting to 1.28 Å resolution
Author(s) -
Ostermeier Christian,
Essen LarsOliver,
Michel Hartmut
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340210110
Subject(s) - resolution (logic) , orthorhombic crystal system , integral membrane protein , crystallography , chemistry , paracoccus denitrificans , fragment (logic) , escherichia coli , protein crystallization , analytical chemistry (journal) , membrane , membrane protein , crystal structure , crystallization , chromatography , biochemistry , enzyme , gene , organic chemistry , artificial intelligence , programming language , computer science
The F v fragment of a monoclonal antibody, 7E2 (IgG 1 , κ, murine), which is directed against the integral membrane protein cytochrome c oxidase (EC 1.9.3.1) from Paracoccus denitrificans , was cloned and produced in Escherichia coli . Crystals suitable for highresolution X‐ray analysis were obtained by microdialysis under low salt conditions. The crystals belong to the orthorhombic space group P2 1 2 1 2 1 with unit cell dimensions of a = 51.51 Å, b = 56.15 Å, c = 99.86 Å (1 Å = 0.1 nm) and contain one F v fragment per asymmetric unit. Using synchrotron radiation diffraction data were collected up to 1.28 Å resolution. This high resolution is very unusual for a heterodimeric protein. The crystals should open the way for refining not only the atomic positions, but also for obtaining information about internal dynamics. © 1995 Wiley‐Liss, Inc.