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.
| 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 | |
| State | Published - Jul 2 1988 |
Funding
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.).
ASJC Scopus subject areas
- Condensed Matter Physics
- Inorganic Chemistry
- Materials Chemistry