Publications by authors named "S M Soltis"

This study takes an affiliative coping theory perspective to examine whether working adults reactivated dormant ties with individuals they had not contacted for at least 3 years to cope with stressors experienced due to the COVID-19 pandemic. Stressors originating in the workplace (job insecurity and remote work) and in the family (stressful familial social ties) were examined in a sample of 232 working adults in the southeastern United States. Individuals were more likely to reactivate their dormant ties when their job was insecure, and the magnitude of the reactivations was greater among individuals experiencing stressful social ties with family members than those not experiencing those stressors.

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Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable 6 orders of magnitude.

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Article Synopsis
  • Deoxynucleotide triphosphohydrolases (dNTPases) like dGTPase are essential for maintaining dNTP pools, influencing cellular survival and DNA replication, with dGTPase being unique in specifically hydrolyzing dGTP.
  • The researchers used advanced techniques to reveal the free and bound structures of dGTPase, demonstrating how the enzyme's active site is dynamic and undergoes conformational changes when dGTP binds, while an inhibitor (GTP) keeps it in an inactive state.
  • Despite similarities between dGTPase and other enzymes like SAMHD1, dGTPase has unique features that confer guanine base specificity and the ability to enhance
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The nicotinamide nucleotide transhydrogenase (TH) is an integral membrane enzyme that uses the proton-motive force to drive hydride transfer from NADH to NADP in bacteria and eukaryotes. Here we solved a 2.2-Å crystal structure of the TH transmembrane domain (Thermus thermophilus) at pH 6.

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X-ray free-electron lasers (XFELs) provide very intense X-ray pulses suitable for macromolecular crystallography. Each X-ray pulse typically lasts for tens of femtoseconds and the interval between pulses is many orders of magnitude longer. Here we describe two novel acoustic injection systems that use focused sound waves to eject picoliter to nanoliter crystal-containing droplets out of microplates and into the X-ray pulse from which diffraction data are collected.

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