Refined structure of alkaline phosphatase from Escherichia coli at 2.8 Å resolution
- 1 November 1985
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 186 (2), 417-433
- https://doi.org/10.1016/0022-2836(85)90115-9
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Crystallographic observations of the metal ion triple in the active site region of alkaline phosphataseJournal of Molecular Biology, 1983
- Refined crystal structure of carboxypeptidase a at 1·54 Å resolutionJournal of Molecular Biology, 1983
- Structure of alkaline phosphatase with zinc/magnesium cobalt or cadmium in the functional metal sitesJournal of Molecular Biology, 1981
- Packing of α-Helices onto β-Pleated sheets and the anatomy of proteinsJournal of Molecular Biology, 1980
- Relation between structure and function of α/β–protejnsQuarterly Reviews of Biophysics, 1980
- Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenasesJournal of Molecular Biology, 1978
- Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphataseNature, 1978
- A crystallographic study of alkaline phosphatase at 7.7 Å resolutionJournal of Molecular Biology, 1973
- The interpretation of protein structures: Estimation of static accessibilityJournal of Molecular Biology, 1971
- The detection of sub-units within the crystallographic asymmetric unitActa Crystallographica, 1962