Related Experiment Video
Updated: Jul 30, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Association behaviour of human betaB1-crystallin and its truncated forms
O A Bateman1, N H Lubsen, C Slingsby
1Birkbeck College, Department of Crystallography, Malet Street, London, WC1E 7HX, UK.
Abstract:
betaB1-crystallin plays an important role in the assembly of betaH-crystallin yet is known to be subject to N-terminal sequence truncations during human lens development and ageing. Here we have over-expressed human betaB1-crystallin, and various truncated forms in Escherichia coli and used mass spectrometry to monitor the monomer molecular weight. Gel permeation chromatography and laser light scattering have been used to estimate the assembly size of the various polypeptides as a function of protein concentration. The full-length betaB1-crystallin behaves as a dimer, like recombinant human betaB2-crystallin, but undergoes further self-association at high protein concentrations, unlike the betaB2-crystallin. Major truncations from the N-terminal extension lead to anomalous behaviour on gel permeation chromatography indicative of altered interactions with the column matrix, whereas light scattering indicated dimers at low protein concentration that self-associate as a function of protein concentration. Loss of 41 residues from the N-terminus, equivalent to an in vivo truncation site, resulted in temperature-dependent phase separation behaviour of the shortened betaB1-crystallin. Good crystals have been grown of a truncated version of human betaB1-crystallin using an in vitro cleavage protocol.
More Related Videos
09:31PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
Published on: September 26, 2020
06:47ABCG5/G8 Crystallization in a Lipidic Bicelle Environment for X-Ray Crystallography
Published on: August 25, 2023
Related Concept Videos
Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...