Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Ingo Kölln"'
Autor:
Maggie Kessler, Daniela Janell, Anat Bashan, Frank Schlünzen, Marco Glühmann, Ante Tocilj, J. Harms, Harly A. S. Hansen, Heike Bartels, Francois Franceschi, Tamar Auerbach, Moshe Peretz, Ilana Agmon, W. S. Bennett, Shulamith Weinstein, Inna Levin, Horacio Avila, Ada Yonath, Marta Pioletti, Susanne Krumbholz, Kostas Anagnostopoulos, Ingo Kölln
Publikováno v:
Journal of Synchrotron Radiation. 6:928-941
Crystals of small and large ribosomal subunits from thermophilic and halophilic bacteria, diffracting to 3 A, are being subjected to structural analysis with synchrotron radiation. The bright beam necessary for detecting and collecting the diffractio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::020b98e9f009dce18182539dbfd3a5f6
https://doi.org/10.1107/s0909049599006664
https://doi.org/10.1107/s0909049599006664
Autor:
Juan J. Calvete, Antonio A. Romero, João M. Dias, Paloma F. Varela, Ana Luísa Carvalho, Edda Töpfer-Petersen, Maria João Romão, Libia Sanz, Ingo Kölln
Publikováno v:
Journal of Molecular Biology. 274:650-660
We report the three-dimensional crystal structure of acidic seminal fluid protein (aSFP), a 12.9 kDa polypeptide of the spermadhesin family isolated from bovine seminal plasma, solved by the multiple isomorphous replacement method and refined with da
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c951e676cba2226c91ca3dddcb600629
https://doi.org/10.1006/jmbi.1997.1423
https://doi.org/10.1006/jmbi.1997.1423
Autor:
Heike Bartels, Francois Franceshi, Ilana Agmon, Ante Tocilj, Harly A. S. Hansen, Anat Bashan, Ada Yonath, Marco Glühmann, Maggie Kessler, Ingo Kölln, Daniela Janell, Shulamith Weinstein, J. Harms, Frank Schlünzen
Publikováno v:
Polyoxometalate Chemistry From Topology via Self-Assembly to Applications ISBN: 0792370112
Heteropolytungstates play a dual role in ribosomal crystallography. Beside generating phases, one of them, (NH4)6(P2W18O62)14H2O, was found to be extremely useful in inducing post crystallization rearrangements. These led to a significant increase in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c0b108d10e8f4ec4e9e821cf0f942322
https://doi.org/10.1007/0-306-47625-8_25
https://doi.org/10.1007/0-306-47625-8_25
Autor:
Antonio A. Romero, Paloma F. Varela, João Miguel L. Dias, Maria João Romão, Ana Luísa Carvalho, Ingo Kölln, Edda Töpfer-Petersen, Juan J. Calvete, Claus Urbanke
Publikováno v:
Protein Science. 6:725-727
Bovine acidic seminal fluid protein (aSFP) is a 1.29 kDa polypeptide of the spermadhesin family built by a single CUB domain architecture. The CUB domain is an extracellular module present in 16 functionally diverse proteins. To determine the three-d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b899956bdb12d02e413a055ba9c1f218
https://doi.org/10.1002/pro.5560060323
https://doi.org/10.1002/pro.5560060323
Autor:
Moshe Peretz, Werner Jahn, Horacio Avila, C. Glotz, Ilana Agmon, Inna Levin, Anat Bashan, Maggie Kessler, Tamar Auerbach, Shulamith Weinstein, Frank Schlünzen, Marco Glühmann, Marta Pioletti, Heike Bartels, Francois Franceschi, Kostas Anagnostopoulos, Ingo Kölln, Harly A. S. Hansen, J. Harms, Ada Yonath, Daniela Janell, W. S. Bennett
Publikováno v:
Journal of structural biology. 127(2)
Procedures were developed exploiting organometallic clusters and coordination compounds in combination with heavy metal salts for derivatization of ribosomal crystals. These enabled the construction of multiple isomorphous replacement (MIR) and multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75d0f84ca2c42058f5780b824949f1bc
https://pubmed.ncbi.nlm.nih.gov/10527903
https://pubmed.ncbi.nlm.nih.gov/10527903
Autor:
Ante Tocilj, Holger Stark, Anat Bashan, Ada Yonath, Inna Levin, J. Harms, Ingo Kölln, Frank Schlünzen, Ilana Agmon, Francois Franceschi, Marianne E. Cuff, Marin van Heel
Publikováno v:
Structure Folding and Design
Background: Ribosomes are the universal cellular organelles that accomplish the translation of the genetic code into proteins. Electron cryo-microscopy (cryo-EM) has yielded fairly detailed three-dimensional reconstructions of ribosomes. These were u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64eaac26eaee2a7e49c5e765e6f96fa7
https://pubmed.ncbi.nlm.nih.gov/10467138
https://pubmed.ncbi.nlm.nih.gov/10467138
Autor:
Ingo Kölln, Maria João Romão, Libia Sanz, Juan J. Calvete, Ana Luísa Carvalho, Edda Töpfer-Petersen, João M. Dias, Paloma F. Varela, Antonio Romero
Publikováno v:
CIÊNCIAVITAE
Scopus-Elsevier
Scopus-Elsevier
Spermadhesins, 12,000-14,000 M(r) mammalian proteins, include lectins involved in sperm-egg binding and display a single CUB domain architecture. We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e90c5856f77b582c953b947fd10999
https://pubmed.ncbi.nlm.nih.gov/9334740
https://pubmed.ncbi.nlm.nih.gov/9334740