Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Michael C. Merckel"'
Autor:
Pasi Laurinmäki, Michael C. Merckel, Ritva Serimaa, Teemu P. Ikonen, Roman Tuma, Jakub Pšenčík, Sarah J. Butcher
Publikováno v:
Biophysical Journal. 87:1165-1172
Chlorosomes of green photosynthetic bacteria constitute the most efficient light harvesting complexes found in nature. In addition, the chlorosome is the only known photosynthetic system where the majority of pigments (BChl) is not organized in pigme
Autor:
Jack C. Leo, Michael C. Merckel, Hilkka Lankinen, Heli Nummelin, Mikael Skurnik, Adrian Goldman
Publikováno v:
The EMBO Journal. 23:701-711
The crystal structure of the recombinant collagen-binding domain of Yersinia adhesin YadA from Yersinia enterocolitica serotype O:3 was solved at 1.55 A resolution. The trimeric structure is composed of head and neck regions, and the collagen binding
The Structural Basis of Receptor-binding by Escherichia coli Associated with Diarrhea and Septicemia
Autor:
Michael C. Merckel, Jarna Tanskanen, Adrian Goldman, Sanna Edelman, Benita Westerlund-Wikström, Timo K. Korhonen
Publikováno v:
Journal of Molecular Biology. 331:897-905
GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal disease, and the structure of the ligand-binding domain, GafD1-178, has been determined at 1.7 A resolution in the presence of the receptor sugar N -acetyl- d -glucosamine. The ov
Autor:
Sandra Falck, Pekka Lappalainen, Matthias Wilmanns, Michael C. Merckel, Pauli J. Ojala, Ville O. Paavilainen, Ehmke Pohl
Publikováno v:
Journal of Biological Chemistry. 277:43089-43095
Twinfilin is an evolutionarily conserved actin monomer-binding protein that regulates cytoskeletal dynamics in organisms from yeast to mammals. It is composed of two actin-depolymerization factor homology (ADF-H) domains that show approximately 20% s
Autor:
Michael C. Merckel, Anu Salminen, Reijo Lahti, Nisse Kalkkinen, Adrian Goldman, Igor P. Fabrichniy, Alexander A. Baykov
Publikováno v:
Structure. 9(4):289-297
Background: Streptococcus mutans pyrophosphatase (Sm-PPase) is a member of a relatively uncommon but widely dispersed sequence family (family II) of inorganic pyrophosphatases. A structure will answer two main questions: is it structurally similar to
Autor:
David L. Ollis, John W. Kozarich, Adrian Goldman, Veli-Matti Leppänen, Kenny K. Wong, Michael C Merckel
Publikováno v:
Structure. 7:733-744
Background: Pyruvate formate lyase (PFL) catalyses a key step in Escherichia coli anaerobic glycolysis by converting pyruvate and CoA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate, involving an essential
Publikováno v:
Structure. 5(5):635-646
Background: Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth temperature 98°C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyot
Autor:
Paul Gottlieb, Hassan Belrhali, Hui Wei, Denis E. Kainov, Dennis H. Bamford, Roman Tuma, Michael C. Merckel, Vladimir M. Simonov, Martin A. Walsh
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 60(Pt 12 Pt 2)
Bacteriophage varphi12 protein P7 is a structural component of the polymerase complex and ensures stable packaging of the genomic RNA. varphi12 P7 has been cloned, purified and crystallized. Crystals belong to space group P3(2)21, with unit-cell para
Autor:
Pauli Ollikka, Yasmin El Tahir, Heli Nummelin, Michael C. Merckel, Adrian Goldman, Mikael Skurnik
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9780306477591
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::420d4a6ba37a9d10d8753284063d9f0a
https://doi.org/10.1007/0-306-48416-1_15
https://doi.org/10.1007/0-306-48416-1_15
Autor:
Nisse Kalkkinen, Adrian Goldman, J. Günter Grossmann, Michael C. Merckel, Andrew Thompson, Ashley M. Deacon, Tommi Kajander
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 58(Pt 5)
The structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Neurospora crassa was determined at 3.0 A resolution. Phase information was derived from a multiwavelength anomalous dispersion (MAD) experiment conducted at three wavelengths using