Structures of d-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and d-sorbitol at 2.5 Å and 2.3 Å resolution, respectively
- 1 July 1989
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 208 (1) , 129-157
- https://doi.org/10.1016/0022-2836(89)90092-2
Abstract
No abstract availableThis publication has 71 references indexed in Scilit:
- Helix geometry in proteinsPublished by Elsevier ,2004
- Hydrogen bonding in globular proteinsPublished by Elsevier ,2003
- The crystallization of glucose isomerase from Arthrobacter B3728Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactionsJournal of Molecular Biology, 1981
- A new least-squares refinement technique based on the fast Fourier transform algorithmActa Crystallographica Section A, 1978
- Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 ÅJournal of Molecular Biology, 1978
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975
- Parameter refinement in the multiple isomorphous-replacement methodActa Crystallographica Section A, 1973
- Refinement of bond angles of an α-helixJournal of Molecular Biology, 1967
- The treatment of errors in the isomorphous replacement methodActa Crystallographica, 1959