| Literature DB >> 31204690 |
Patricia S Langan1, Venu Gopal Vandavasi1, Brendan Sullivan1, Joel Harp2, Kevin Weiss1, Leighton Coates1.
Abstract
The mechanism by which potassium ions are transported through ion channels is currently being investigated by several groups using many different techniques. Clarification of the location of water molecules during transport is central to understanding how these integral membrane proteins function. Neutrons have a unique sensitivity to both hydrogen and potassium, rendering neutron crystallography capable of distinguishing waters from K+ ions. Here, the collection of a complete neutron data set from a potassium ion channel to a resolution of 3.55 Å using the Macromolecular Neutron Diffractometer (MaNDi) is reported. A room-temperature X-ray data set was also collected from the same crystal to a resolution of 2.50 Å. Upon further refinement, these results will help to further clarify the ion/water population within the selectivity filter of potassium ion channels.Entities:
Keywords: X-ray diffraction; ion channels; membrane proteins; neutron diffraction
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Year: 2019 PMID: 31204690 PMCID: PMC6572099 DOI: 10.1107/S2053230X19006630
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056