Related Experiment Video
Updated: Aug 8, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Improving the quality of protein crystals through purification by isoelectric focusing
Abstract:
Preparative flat-bed gel isoelectric focusing has reduced or eliminated observed heterogeneity in three different proteins, thereby greatly improving the quality of crystals grown from each of them. This improvement is manifested both in crystal size and in increased measurability of diffraction data. Isoelectric focusing is a general and nondestructive technique that may facilitate the crystallographic study of proteins which are biologically interesting, but which, for reasons of microheterogeneity, do not yield diffraction quality crystals.
More Related Videos
10:21Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
09:57Separation of Bioactive Small Molecules, Peptides from Natural Sources and Proteins from Microbes by Preparative Isoelectric Focusing (IEF) Method
Published on: June 14, 2020
Related Concept Videos
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Two-dimensional Gel Electrophoresis
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...