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0562970 - BTÚ 2023 RIV DK eng J - Journal Article
Adámková, Kristýna - Koval, Tomáš - Ostergaard, L. H. - Dušková, Jarmila - Malý, Martin - Švecová, Leona - Skálová, Tereza - Kolenko, Petr - Dohnálek, Jan
Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects.
Acta Crystallographica Section D-Biological Crystallography. Roč. 78, OCT 1 2022 (2022), s. 1194-1209. ISSN 1399-0047. E-ISSN 2059-7983
R&D Projects: GA MŠMT(CZ) LM2015043; GA MŠMT(CZ) LM2018127; GA ČR(CZ) GA20-12109S; GA MŠMT EF15_003/0000447
Institutional support: RVO:86652036
Keywords : S1 nuclease * Aspergillus oryzae * lattice-translocation defects * nucleotides * nucleosides * complexes
OECD category: Analytical chemistry
Impact factor: 2.2, year: 2022
Method of publishing: Limited access
https://scripts.iucr.org/cgi-bin/paper?S2059798322008397
Permanent Link: https://hdl.handle.net/11104/0340705