| ADAMKOVA, Kristyna, Tomas KOVAL, Lars H OSTERGAARD, Jarmila DUSKOVA, Martin MALY, Leona SVECOVA, Tereza SKALOVA, Petr KOLENKO and Jan DOHNALEK. Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects. Acta Crystallographica Section D: Structural Biology. Chester: International Union of Crystallography, 2022, vol. 78, OCT, p. 1194-1209. ISSN 2059-7983. Available from: https://dx.doi.org/10.1107/S2059798322008397. |
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@article{2262420,
author = {Adamkova, Kristyna and Koval, Tomas and Ostergaard, Lars H and Duskova, Jarmila and Maly, Martin and Svecova, Leona and Skalova, Tereza and Kolenko, Petr and Dohnalek, Jan},
article_location = {Chester},
article_number = {OCT},
doi = {http://dx.doi.org/10.1107/S2059798322008397},
keywords = {S1 nuclease; Aspergillus oryzae; lattice-translocation defects; nucleotides; nucleosides; complexes},
language = {eng},
issn = {2059-7983},
journal = {Acta Crystallographica Section D: Structural Biology},
title = {Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects},
url = {https://scripts.iucr.org/cgi-bin/paper?S2059798322008397},
volume = {78},
year = {2022}
}
TY - JOUR
ID - 2262420
AU - Adamkova, Kristyna - Koval, Tomas - Ostergaard, Lars H - Duskova, Jarmila - Maly, Martin - Svecova, Leona - Skalova, Tereza - Kolenko, Petr - Dohnalek, Jan
PY - 2022
TI - Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects
JF - Acta Crystallographica Section D: Structural Biology
VL - 78
IS - OCT
SP - 1194-1209
EP - 1194-1209
PB - International Union of Crystallography
SN - 20597983
KW - S1 nuclease
KW - Aspergillus oryzae
KW - lattice-translocation defects
KW - nucleotides
KW - nucleosides
KW - complexes
UR - https://scripts.iucr.org/cgi-bin/paper?S2059798322008397
N2 - S1 nuclease from Aspergillus oryzae is a single-strand-specific nuclease from the S1/P1 family that is utilized in biochemistry and biotechnology. S1 nuclease is active on both RNA and DNA but with differing catalytic efficiencies. This study clarifies its catalytic properties using a thorough comparison of differences in the binding of RNA and DNA in the active site of S1 nuclease based on X-ray structures, including two newly solved complexes of S1 nuclease with the products of RNA cleavage at atomic resolution. Conclusions derived from this comparison are valid for the whole S1/P1 nuclease family. For proper model building and refinement, multiple lattice-translocation defects present in the measured diffraction data needed to be solved. Two different approaches were tested and compared. Correction of the measured intensities proved to be superior to the use of the dislocation model of asymmetric units with partial occupancy of individual chains. As the crystals suffered from multiple lattice translocations, equations for their correction were derived de novo. The presented approach to the correction of multiple lattice-translocation defects may help to solve similar problems in the field of protein X-ray crystallography.
ER -
ADAMKOVA, Kristyna, Tomas KOVAL, Lars H OSTERGAARD, Jarmila DUSKOVA, Martin MALY, Leona SVECOVA, Tereza SKALOVA, Petr KOLENKO and Jan DOHNALEK. Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects. \textit{Acta Crystallographica Section D: Structural Biology}. Chester: International Union of Crystallography, 2022, vol.~78, OCT, p.~1194-1209. ISSN~2059-7983. Available from: https://dx.doi.org/10.1107/S2059798322008397.
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