M F Symmons
Affiliation: University of Cambridge
- A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulationM F Symmons
Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom
Structure 8:1215-26. 2000..Streptomyces antibioticus PNPase also assays as a guanosine 3'-diphosphate 5'-triphosphate (pppGpp) synthetase (E.C.220.127.116.11). It may function to coordinate changes in mRNA lifetimes with pppGpp levels during the Streptomyces lifecycle...
- Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membraneD A Marvin
Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK
J Mol Biol 355:294-309. 2006..Here we show that reinterpreted NMR data are also consistent with the model derived from X-ray fibre diffraction studies, and discuss models of virion assembly...
- On the structures of filamentous bacteriophage Ff (fd, f1, M13)S K Straus
Department of Chemistry, University of British Columbia, Vancouver, BC, Canada
Eur Biophys J 37:521-7. 2008..We suggest possible reasons for the differences between the models derived from cryoEM and X-ray diffraction...