Malwina Radwanska
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Malwina Radwanska has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
- Daniel A. Engel
Department of Microbiology, Immunology and Cancer Biology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA
1 shared publication - Malgorzata Bukrejewska
Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA
1 shared publication - Urszula Derewenda
Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA
1 shared publication - Zygmunt Stanislaw Derewenda
Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA
1 shared publication
Latest Publications
- 15 August 2017
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D Structural Biology
- Vol. 73 (9) , 767-774
Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain
Two nonstructural proteins encoded byZika virusstrain MR766 RNA, a methyltransferase and a helicase, were crystallized and their structures were solved and refined at 2.10 and 2.01 Å resolution, respectively. The NS5 methyltransferase contains a boundS-adenosyl-L-methionine (SAM) co-substrate. The NS3 helicase is in the apo form. Comparison with published crystal structures of the helicase in the apo, nucleotide-bound and single-stranded RNA (ssRNA)-bound states suggests that binding of ssRNA to the helicase may occur through conformational selection rather than induced fit.
- 15 August 2017
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D Structural Biology
- Vol. 73 (9) , 767-774
Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain
Two nonstructural proteins encoded byZika virusstrain MR766 RNA, a methyltransferase and a helicase, were crystallized and their structures were solved and refined at 2.10 and 2.01 Å resolution, respectively. The NS5 methyltransferase contains a boundS-adenosyl-L-methionine (SAM) co-substrate. The NS3 helicase is in the apo form. Comparison with published crystal structures of the helicase in the apo, nucleotide-bound and single-stranded RNA (ssRNA)-bound states suggests that binding of ssRNA to the helicase may occur through conformational selection rather than induced fit.