Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution
- 1 August 1991
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 220 (4) , 975-994
- https://doi.org/10.1016/0022-2836(91)90367-f
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Helix geometry in proteinsPublished by Elsevier ,2004
- Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium contentJournal of Molecular Biology, 1989
- Mechanisms of flavoprotein‐catalyzed reactionsEuropean Journal of Biochemistry, 1989
- Testing the method of crystallographic refinement using molecular dynamicsJournal of Applied Crystallography, 1989
- Crystallographic R Factor Refinement by Molecular DynamicsScience, 1987
- New flavins for old: artificial flavins as active site probes of flavoproteinsBiochemical Journal, 1986
- The role of the α-helix dipole in protein function and structureProgress in Biophysics and Molecular Biology, 1985
- The composition of the pyruvate dehydrogenase complex from Azotobacter vinelandiiEuropean Journal of Biochemistry, 1984
- A new least-squares refinement technique based on the fast Fourier transform algorithmActa Crystallographica Section A, 1978
- The α-helix dipole and the properties of proteinsNature, 1978