Publications by authors named "D F WATERMAN"

The Guest Editors introduce the special issue based on talks at the CCP4 Study Weekend 2023. The virtual issue is available at https://journals.iucr.

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Cells evoke the DNA damage checkpoint (DDC) to inhibit mitosis in the presence of DNA double-strand breaks (DSBs) to allow more time for DNA repair. In budding yeast, a single irreparable DSB is sufficient to activate the DDC and induce cell cycle arrest prior to anaphase for about 12-15 hr, after which cells 'adapt' to the damage by extinguishing the DDC and resuming the cell cycle. While activation of the DNA damage-dependent cell cycle arrest is well understood, how it is maintained remains unclear.

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The DIALS package provides a set of tools for crystallographic data processing. The open-source nature of the project, and a flexible interface in which individual command-line programs each have a dedicated job, have enabled the adaptation of DIALS to a wide range of experiment types, including electron diffraction. Here we present detailed instructions for the use of DIALS to process chemical crystallography diffraction data from continuous rotation electron diffraction experiments.

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Article Synopsis
  • The Covid-19 pandemic accelerated the adoption of virtual consultations in healthcare, and this study investigates the use of both virtual and face-to-face formats for palliative care post-pandemic.
  • A mixed-methods approach was utilized, involving an online survey of palliative care physicians and qualitative interviews with patients and caregivers to gather insights on their experiences and preferences regarding consultation formats.
  • The results indicated a preference for face-to-face consultations for physical exams and initial visits, while video consultations were favored for stable symptoms, highlighting the benefits of a blended approach that enhances flexibility and reduces travel burdens for patients and caregivers.
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Detoxification of heme in depends on its crystallization into hemozoin. This pathway is a major target of antimalarial drugs. The crystalline structure of hemozoin was established by X-ray powder diffraction using a synthetic analog, β-hematin.

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