The importance of purity in the crystallization of DNA binding immunoglobulin Fab fragments

Wayne F. Anderson; Amechand Boodhoo; Clifford D. Mol

doi:10.1016/0022-0248(88)90310-7

The importance of purity in the crystallization of DNA binding immunoglobulin F_ab fragments

Wayne F. Anderson^*, Amechand Boodhoo, Clifford D. Mol

^*Corresponding author for this work

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

As part of a program to determine the structures of a number of immunoglobulin F_ab fragments that are specific for different DNA structures or sequences, the affects of sample purity upon crystallization have been studied. The protease treatment utilized to produce F_ab fragments introduces micro-heterogeneity into the sample which is detrimental to crystal growth. Purification of a single F_ab species was found to be an essential step in obtaining large single crystals. If crystallization experiments on biological macromolecules yield only microcrystals or if crystallization is not reproducible the most likely causes for these problems are insufficient purity of the sample and variation in the level of purity.

Original language	English (US)
Pages (from-to)	153-159
Number of pages	7
Journal	Journal of Crystal Growth
Volume	90
Issue number	1-3
DOIs	https://doi.org/10.1016/0022-0248(88)90310-7
State	Published - Jul 2 1988

ASJC Scopus subject areas

Condensed Matter Physics
Inorganic Chemistry
Materials Chemistry

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10.1016/0022-0248(88)90310-7

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title = "The importance of purity in the crystallization of DNA binding immunoglobulin Fab fragments",

abstract = "As part of a program to determine the structures of a number of immunoglobulin Fab fragments that are specific for different DNA structures or sequences, the affects of sample purity upon crystallization have been studied. The protease treatment utilized to produce Fab fragments introduces micro-heterogeneity into the sample which is detrimental to crystal growth. Purification of a single Fab species was found to be an essential step in obtaining large single crystals. If crystallization experiments on biological macromolecules yield only microcrystals or if crystallization is not reproducible the most likely causes for these problems are insufficient purity of the sample and variation in the level of purity.",

author = "Anderson, {Wayne F.} and Amechand Boodhoo and Mol, {Clifford D.}",

note = "Funding Information: The authors would like to acknowledge the very helpful collaboration with Jeremy S. Lee, programming assistance and computer programs from David Bacon and John Moult and helpful discussions with Mirek Cygler and Alastair Muir. This work was supported by the Medical Research Council of Canada through the MRC Group on Protein Structure and Function and by a graduate fellowship from the Alberta Heritage Foundation for Medical research (to C.D.M.).",

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AU - Anderson, Wayne F.

AU - Boodhoo, Amechand

AU - Mol, Clifford D.

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PY - 1988/7/2

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N2 - As part of a program to determine the structures of a number of immunoglobulin Fab fragments that are specific for different DNA structures or sequences, the affects of sample purity upon crystallization have been studied. The protease treatment utilized to produce Fab fragments introduces micro-heterogeneity into the sample which is detrimental to crystal growth. Purification of a single Fab species was found to be an essential step in obtaining large single crystals. If crystallization experiments on biological macromolecules yield only microcrystals or if crystallization is not reproducible the most likely causes for these problems are insufficient purity of the sample and variation in the level of purity.

AB - As part of a program to determine the structures of a number of immunoglobulin Fab fragments that are specific for different DNA structures or sequences, the affects of sample purity upon crystallization have been studied. The protease treatment utilized to produce Fab fragments introduces micro-heterogeneity into the sample which is detrimental to crystal growth. Purification of a single Fab species was found to be an essential step in obtaining large single crystals. If crystallization experiments on biological macromolecules yield only microcrystals or if crystallization is not reproducible the most likely causes for these problems are insufficient purity of the sample and variation in the level of purity.

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The importance of purity in the crystallization of DNA binding immunoglobulin F_ab fragments

Abstract

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