{"entity": "researcher", "timestamp": "2026-10-01T12:33:47.898Z", "family": "Andersson", "given": "M", "initials": "M", "orcid": "0000-0002-3364-6647", "affiliations": ["Science for Life Laboratory, Department of Physics and Swedish e-Science Research Center, KTH Royal Institute of Technology, Solna, SE-171 21, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/36cb60bd233148b9a73c311b41bf32fc.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/36cb60bd233148b9a73c311b41bf32fc"}}, "publications": [{"entity": "publication", "iuid": "1c49afd9b7a349dca3b28ffba23c5943", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1c49afd9b7a349dca3b28ffba23c5943.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1c49afd9b7a349dca3b28ffba23c5943"}}, "title": "Probing the activity of a recombinant Zn2+ -transporting P-type ATPase.", "authors": [{"family": "Ravishankar", "given": "H", "initials": "H"}, {"family": "Barth", "given": "A", "initials": "A"}, {"family": "Andersson", "given": "M", "initials": "M", "orcid": "0000-0002-3364-6647", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/36cb60bd233148b9a73c311b41bf32fc.json"}}], "type": "journal article", "published": "2018-02-00", "journal": {"title": "Biopolymers", "issn": "1097-0282", "volume": "109", "issue": "2", "issn-l": "0006-3525"}, "abstract": "P-type ATPase proteins maintain cellular homeostasis and uphold critical concentration gradients by ATP-driven ion transport across biological membranes. Characterization of single-cycle dynamics by time-resolved X-ray scattering techniques in solution could resolve structural intermediates not amendable to for example crystallization or cryo-electron microscopy sample preparation. To pave way for such time-resolved experiments, we used biochemical activity measurements, Attenuated Total Reflectance (ATR) and time-dependent Fourier-Transform Infra-Red (FTIR) spectroscopy to identify optimal conditions for activating a Zn2+ -transporting Type-I ATPase from Shigella sonnei (ssZntA) at high protein concentration using caged ATP. The highest total activity was observed at a protein concentration of 25 mg/mL, at 310 K, pH 7, and required the presence of 20% (v/v) glycerol as stabilizing agent. Neither the presence of caged ATP nor increasing lipid-to-protein ratio affected the hydrolysis activity significantly. This work also paves way for characterization of recombinant metal-transporting (Type-I) ATPase mutants with medical relevance.", "doi": "10.1002/bip.23087", "pmid": "29168553", "labels": [], "xrefs": [], "notes": [], "created": "2018-12-05T12:44:44.404Z", "modified": "2026-09-23T12:22:32.250Z"}]}