Found: 17
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Tetracycline‐modifying enzyme SmTetX from Stenotrophomonas maltophilia.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2023, v. 79, n. 7, p. 180, doi. 10.1107/S2053230X23005381
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- Article
Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse.
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- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-32577-6
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- Article
Crystallization of nepenthesin I using a low-pH crystallization screen.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2016, v. 72, n. 1, p. 24, doi. 10.1107/S2053230X15022323
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Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2015, v. 71, n. 11, p. 1408, doi. 10.1107/S2053230X15018324
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- Article
Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.
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- Nucleic Acids Research, 2014, v. 42, n. 8, p. 5151
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- Article
A highly active S1‐P1 nuclease from the opportunistic pathogen Stenotrophomonas maltophilia cleaves c‐di‐GMP.
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- FEBS Letters, 2023, v. 597, n. 16, p. 2103, doi. 10.1002/1873-3468.14683
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- Article
The first structure–function study of GH151 α‐l‐fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity.
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- FEBS Journal, 2022, v. 289, n. 16, p. 4998, doi. 10.1111/febs.16387
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- Article
Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
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- Scientific Reports, 2019, v. 9, n. 1, p. N.PAG, doi. 10.1038/s41598-019-50105-3
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- Article
Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice‐translocation defects.
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- Acta Crystallographica: Section D, Structural Biology, 2022, v. 78, n. 10, p. 1194, doi. 10.1107/S2059798322008397
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- Article
Crystallographic fragment screening‐based study of a novel FAD‐dependent oxidoreductase from Chaetomium thermophilum. Corrigendum.
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- Acta Crystallographica: Section D, Structural Biology, 2021, v. 77, n. 7, p. 980, doi. 10.1107/S2059798321006100
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- Article
Crystallographic fragment screening‐based study of a novel FAD‐dependent oxidoreductase from Chaetomium thermophilum.
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- Acta Crystallographica: Section D, Structural Biology, 2021, v. 77, n. 6, p. 755, doi. 10.1107/S2059798321003533
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- Article
SHELIXIR: automation of experimental phasing procedures using SHELXC/D/E.
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- Journal of Applied Crystallography, 2021, v. 54, n. 3, p. 996, doi. 10.1107/S1600576721002454
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Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non–Specificity, and Inhibition.
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- PLoS ONE, 2016, v. 11, n. 12, p. 1, doi. 10.1371/journal.pone.0168832
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Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase.
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- FEBS Letters, 2019, v. 593, n. 9, p. 996, doi. 10.1002/1873-3468.13385
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- Article
Active site complementation and hexameric arrangement in the GH family 29; a structure–function study of α-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus.
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- Glycobiology, 2019, v. 29, n. 1, p. 59, doi. 10.1093/glycob/cwy078
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Structure analysis of group I plant nucleases.
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- Journal of Synchrotron Radiation, 2011, v. 18, n. 1, p. 29, doi. 10.1107/S0909049510030700
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Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-20158-4
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- Article