X‐ray structures of three interface mutants of γB‐crystallin from bovine eye lens
Author:
Affiliation:
1. Department of Crystallography, Birkbeck College, London WC1E 7HX, United Kingdom
2. Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, D‐93040 Regensburg, Germany
Funder
HCM Network
DFG
Medical Research Council
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.5560070310
Reference44 articles.
1. Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein
2. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins
3. 3D domain swapping: A mechanism for oligomer assembly
4. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II
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