Analysis and optimization of an omnidirectional direction-finding system

System determines the direction of arrival of an electromagnetic wave with the direction information in a readily usable form. It presents a relatively small physical structure and does not require mechanical positioning

A general resonance theory based on Mourre's inequality

We study the perturbation of bound states embedded in the continuous spectrum which are unstable by the Fermi Golden Rule. The approach to resonance theory based on spectral deformation is extended to a more general class of quantum systems characterized by Mourre's inequality and smoothness of the resolvent. Within the framework of perturbation theory it is still possible to give a definite meaning to the notion of complex resonance energies and of corresponding metastable states. The main result is a quasi-exponential decay estimate up to a controlled error of higher order in perturbation theory.Comment: 17 page

The heat kernel expansion for the electromagnetic field in a cavity

We derive the first six coefficients of the heat kernel expansion for the electromagnetic field in a cavity by relating it to the expansion for the Laplace operator acting on forms. As an application we verify that the electromagnetic Casimir energy is finite.Comment: 12 page

Cryo-EM structure of the potassium-chloride cotransporter KCC4 in lipid nanodiscs.

Cation-chloride-cotransporters (CCCs) catalyze transport of Cl- with K+ and/or Na+across cellular membranes. CCCs play roles in cellular volume regulation, neural development and function, audition, regulation of blood pressure, and renal function. CCCs are targets of clinically important drugs including loop diuretics and their disruption has been implicated in pathophysiology including epilepsy, hearing loss, and the genetic disorders Andermann, Gitelman, and Bartter syndromes. Here we present the structure of a CCC, the Mus musculus K+-Cl- cotransporter (KCC) KCC4, in lipid nanodiscs determined by cryo-EM. The structure, captured in an inside-open conformation, reveals the architecture of KCCs including an extracellular domain poised to regulate transport activity through an outer gate. We identify binding sites for substrate K+ and Cl- ions, demonstrate the importance of key coordinating residues for transporter activity, and provide a structural explanation for varied substrate specificity and ion transport ratio among CCCs. These results provide mechanistic insight into the function and regulation of a physiologically important transporter family