@article{ec9b5c8775514353b51d49ef10637a72,
title = "Magnetite-binding proteins from the magnetotactic bacterium: Desulfamplus magnetovallimortis BW-1",
abstract = "Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic Deltaproteobacterium Desulfamplus magnetovallimortis BW-1 identified two new magnetite-binding proteins (Mad10, Mad11). These proteins can be utilized as affinity tags for the immobilization of recombinant fusion proteins to magnetite.",
author = "Anna Pohl and Young, {Sarah A.E.} and Schmitz, {Tara C.} and Daniel Farhadi and Raz Zarivach and Damien Faivre and Blank, {Kerstin G.}",
note = "Funding Information: The authors thank Margit R{\"o}{\ss}ner and Anna-Maria Tsirigoni for help with protein expression and characterization. They further thank the HZB (BESSY II, Helmholtz–Zentrum f{\"u}r Materialien und Energie, Berlin) for the allocation of X-ray synchrotron beam-time and Stefan Siegel and Chenghao Li for technical support. Funding was provided by the International Max Planck Research School on Multiscale Bio-Systems (AP), the Alexander von Humboldt Foundation (RZ) and the Max Planck Society. Open Access funding provided by the Max Planck Society. Publisher Copyright: {\textcopyright} 2021 The Royal Society of Chemistry.",
year = "2021",
month = dec,
day = "28",
doi = "https://doi.org/10.1039/d1nr04870h",
language = "English",
volume = "13",
pages = "20396--20400",
journal = "Nanoscale",
issn = "2040-3364",
publisher = "Royal Society of Chemistry",
number = "48",
}