Zobrazeno 1 - 10
of 43
pro vyhledávání: '"M. Lapkouski"'
Autor:
Antonino Natalello, Ivana Kuta Smatanova, J. Wolfova, Jannette Carey, Rita Grandori, Rüdiger Ettrich, Erin Ebbel, Jiri Brynda, Sy-Yeu Chern, Angela F. Ricci, Neal A. Chatterjee, Michal Kuty, M. Lapkouski, Jeroen R. Mesters
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794:1288-1298
Two previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 A resolution, and new crystals of WrbA apoprotein diffracting to 1.85 A, are refined and analysed comparatively through the lens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7edd8d2f3f32e6eec4ea8b3fe9ad4160
https://doi.org/10.1016/j.bbapap.2009.08.001
https://doi.org/10.1016/j.bbapap.2009.08.001
Autor:
Juan B. Arellano, José L. Revuelta, Rüdiger Ettrich, J. Kohoutová, I. Kuta Smatanova, Jiří Brynda, M. Lapkouski
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Preliminary X-ray diffraction analysis of the extrinsic PsbP protein of photosystem II from spinach (Spinacia oleracea) was performed using N-terminally His-tagged recombinant PsbP protein overexpressed in Escherichia coli. Recombinant PsbP protein (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc94f40e8cb269e1e58ef1ff4a9fd8fa
https://doi.org/10.1107/s1744309108040578
https://doi.org/10.1107/s1744309108040578
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:582-585
EcoR124I is a multicomplex enzyme belonging to the type I restriction-modification system from Escherichia coli. Although EcoR124I has been extensively characterized biochemically, there is no direct structural information available about particular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b4471f1a92776b775d6bc5bf2058a12
https://doi.org/10.1107/s174430910702622x
https://doi.org/10.1107/s174430910702622x
Autor:
Eva Csefalvay, Jannette Carey, Pavel Janscak, Ladislav Csefalvay, Rüdiger Ettrich, Ivana Kuta Smatanova, Alena Guzanova, Katsiaryna Shamayeva, Santosh Panjikar, Marie Weiserova, Vitali Bialevich, M. Lapkouski, Tatsiana Baikova, Igor Shevelev
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 6, p e0128700 (2015)
PLOS ONE
PLoS ONE, Vol 10, Iss 6, p e0128700 (2015)
PLOS ONE
Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on motor subunit HsdR. Functional coupling of DNA cleavage and translocation is a hallmark of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd336ca0e4f0a1444efdbf7d62b982b7
http://europepmc.org/articles/PMC4454674
http://europepmc.org/articles/PMC4454674
Autor:
Olena Sheryemyetyeva, Jiri Brynda, Richard Guerra, Iryna Kishko, Zdenek Kukacka, M. Lapkouski, Petr Novák, Ivana Kuta Smatanova, Michal Kuty, Balasubramanian Harish, Olga Ettrichova, Rüdiger Ettrich, Jannette Carey, Renee Winkler, David Reha
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 69(Pt 9)
The Escherichia coli protein WrbA, an FMN-dependent NAD(P)H:quinone oxidoreductase, was crystallized under new conditions in the presence of FAD or the native cofactor FMN. Slow-growing deep yellow crystals formed with FAD display the tetragonal bipy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::debf4759cc0840f87bf53d022ce283c5
https://pubmed.ncbi.nlm.nih.gov/23999298
https://pubmed.ncbi.nlm.nih.gov/23999298
Autor:
Rüdiger Ettrich, Jaroslava Kohoutova, David Kaftan, Juan B. Arellano, Ivana Kuta Smatanova, Alexander Dulebo, Jannette Carey, Katerina Hofbauerova, José L. Revuelta, M. Lapkouski, Olga Ettrichova, Vladimir Kopecky, Sergio González-Pérez, Zofie Sovova
Publikováno v:
PLoS ONE
PLoS ONE, Vol 7, Iss 10, p e46694 (2012)
Digital.CSIC. Repositorio Institucional del CSIC
instname
PLoS ONE, Vol 7, Iss 10, p e46694 (2012)
Digital.CSIC. Repositorio Institucional del CSIC
instname
This is an open-access article distributed under the terms of the Creative Commons Attribution License.-- et al.
Raman microscopy permits structural analysis of protein crystals in situ in hanging drops, allowing for comparison with Raman measur
Raman microscopy permits structural analysis of protein crystals in situ in hanging drops, allowing for comparison with Raman measur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::382d7cf83ce4531a1ebe9731a4d39df8
https://pubmed.ncbi.nlm.nih.gov/23071614
https://pubmed.ncbi.nlm.nih.gov/23071614
Publikováno v:
Photosynthetica. 47
State transitions in cyanobacteria are physiological adaptation mechanisms that change the interaction of the phycobilisomes with the photosystem I and photosystem II core complexes. This mechanism is essential for cyanobacteria at low light intensit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33c50f961708338f6cebb907b18d5991
https://doi.org/10.1007/s11099-009-0056-x
https://doi.org/10.1007/s11099-009-0056-x
Autor:
Jannette Carey, Ivana Kuta Smatanova, Pavel Janscak, Rüdiger Ettrich, Santosh Panjikar, M. Lapkouski, Eva Csefalvay
Publikováno v:
Nature structuralmolecular biology. 16(1)
Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a2d4a07acc36347a41bd77227807a4e
https://pubmed.ncbi.nlm.nih.gov/19079266
https://pubmed.ncbi.nlm.nih.gov/19079266
Autor:
Marie Weiserova, Igor Shevelev, M. Lapkouski, Eva Csefalvay, Rüdiger Ettrich, Jannette Carey, Ivana Kutá-Smatanová, Pavel Janscak, Tatsiana Baikova
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 65:s135-s135
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::820bde63c19f27d3ed32c2b12a6a7158
https://doi.org/10.1107/s010876730909730x
https://doi.org/10.1107/s010876730909730x
Publikováno v:
Photosynthetica; Sep2009, Vol. 47 Issue 3, p355-362, 8p