Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
- 19 June 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 279 (4), 855-864
- https://doi.org/10.1006/jmbi.1998.1796
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Progress on the Structure and Function of Aquaporin 1Journal of Structural Biology, 1998
- Comparison of the Water Transporting Properties of MIP and AQP1The Journal of Membrane Biology, 1997
- Three-dimensional organization of a human water channelNature, 1997
- MRC Image Processing ProgramsJournal of Structural Biology, 1996
- Aquaporins: water channel proteins of plant and animal cellsTrends in Biochemical Sciences, 1994
- Assembly of 2-D membrane protein crystals: Dynamics, crystal order, and fidelity of structure analysis by electron microscopyJournal of Structural Biology, 1992
- [43] Anion exchange in bacteria: Reconstitution of phosphate: Hexose 6-phosphate antiport from Streptococcus lactisMethods in Enzymology, 1986
- The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloningCell, 1984
- Lens membranes II. Isolation and characterization of the main intrinsic polypeptide (MIP) of bovine lens fiber membranesExperimental Eye Research, 1976
- A study of the structure of the T‐layer of bacillus brevisJournal of Supramolecular Structure, 1973