The 2.8-A resolution structure of the L-arabinose-binding protein from Escherichia coli. Polypeptide chain folding, domain similarity, and probable location of sugar-binding site.
Authors:
- F A QuiochoFQF A Quiocho
- G L GillilandGGG L Gilliland
- G N PhillipsGPG N Phillips
Open Access
- 1 July 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (14) , 5142-5149
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- On the conformation of proteins: The handedness of the β-strand-α-helix-β-strand unitJournal of Molecular Biology, 1976
- Structural patterns in globular proteinsNature, 1976
- The double domain structure of rhodaneseJournal of Molecular Biology, 1975
- Crystallographic data of an l-arabinose-binding protein from Escherichia coliJournal of Molecular Biology, 1974
- Structure of horse muscle phosphoglycerate kinaseJournal of Molecular Biology, 1974
- The matching of physical models to three-dimensional electron-density maps: A simple optical deviceJournal of Molecular Biology, 1968
- Design of a diffractometer and flow cell system for X-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-SJournal of Molecular Biology, 1967
- The structure of carboxypeptidase AJournal of Molecular Biology, 1966
- The crystal structure of myoglobin: Phase determination to a resolution of 2 Å by the method of isomorphous replacementActa Crystallographica, 1961
- The treatment of errors in the isomorphous replacement methodActa Crystallographica, 1959