Počet záznamů: 1
Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidis
- 1.
SYSNO ASEP 0354275 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidis Tvůrce(i) Sviridova, E. (CZ)
Bumba, Ladislav (MBU-M) RID, ORCID
Řezáčová, Pavlína (UMG-J) RID
Procházková, Kateřina (UOCHB-X)
Kavan, Daniel (MBU-M) RID, ORCID
Bezouška, Karel (MBU-M)
Kutý, Michal (UEK-B)
Šebo, Peter (MBU-M) RID, ORCID
Kutá-Smatanová, Ivana (UEK-B) RIDZdroj.dok. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
Roč. 66, - (2010), s. 1119-1123Poč.str. 5 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Fe-regulated protein D ; iron-regulated proteins ; outer membrane lipoproteins Vědní obor RIV EC - Imunologie CEP LC06010 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GP310/06/P150 GA ČR - Grantová agentura ČR CEZ AV0Z50200510 - MBU-M (2005-2011) AV0Z50520514 - UMG-J (2005-2011) AV0Z60870520 - UEK-B (2005-2011) AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000281635600035 DOI 10.1107/S174430911003215X Anotace Fe-regulated protein D (FrpD) is a Neisseria meningitidis outer membrane lipoprotein that may be involved in the anchoring of the secreted repeat in toxins (RTX) protein FrpC to the outer bacterial membrane. However, the function and biological roles of the FrpD and FrpC proteins remain unknown. Native and selenomethionine-subsituted variants of recombinant FrpD43-271 protein were crystalized using the sitting-drop vapour-diffusion method. Diffraction data were collected to a resolution of 2.25 Å for native FrpD43-271 protein and to a resolution of 2.00 Å for selenomethionine-subsitute FrpD43-271 (SeMet FrpD43-271 ) protein. The crystals of native FrdP43-271 protein belonged to the hexagonal space group P62 or P64, while the crystals of SeMet FrpD43-271 protein belonged to the primitive orthorhombic space group P212121 Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2011
Počet záznamů: 1