The N-terminal domain of βb2-crystallin resembles the putative ancestral homodimer
- 1 December 2000
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 304 (3), 253-257
- https://doi.org/10.1006/jmbi.2000.4197
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- The C-terminal domains of gammaS-crystallin pair about a distorted twofold axisProtein Engineering, Design and Selection, 1998
- Molecular evolution of the eye lensProgress in Retinal and Eye Research, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Structural studies on βH-crystallin from bovine eye lensExperimental Eye Research, 1992
- X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteinsNature, 1990
- Short-range order of crystallin proteins accounts for eye lens transparencyNature, 1983
- The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin IINature, 1981
- Theory of Transparency of the EyeApplied Optics, 1971