Structure Characterization of Bacterial Microcompartment Shells via X-ray Scattering and Coordinate Modeling: Evidence for Adventitious Capture of Cytoplasmic Proteins.

Bacterial microcompartments (BMCs) are self-assembling protein shell structures that are widely investigated across a broad range of biological and abiotic chemistry applications. A central challenge in BMC research is the targeted capture of enzymes during shell assembly. While crystallography and cryo-EM techniques have been successful in determining BMC shell structures, there has been only limited success in visualizing the location of BMC-captured enzyme cargo.

Aggressive Serous Carcinomas of the Female Reproductive Tract: Cancer-Prone Cell States and Genetic Drivers.

In 2025, gynecological cancers are projected to account for approximately 10% of cancer-related deaths in women. High-grade serous ovarian carcinoma (HGSC) and serous endometrial carcinoma (SEC) are the most lethal gynecological cancer subtypes. Both malignancies commonly have mutations, alterations of the RB1 pathway, and numerous secondary mutations.

Can we use integrated total pelvic floor ultrasound as a screening tool in defaecatory pelvic floor dysfunction? A prospective evaluation of the accuracy of integrated total pelvic floor ultrasound compared with defaecation proctography.

Aim: Pelvic floor dysfunction is common and includes symptoms such as urinary incontinence, pelvic pain, faecal incontinence, obstructive defaecation syndrome symptoms and pelvic organ prolapse. It is investigated with defaecation proctography (DP) and integrated total pelvic floor ultrasound (TPFUS). Whilst DP is currently the gold standard, TPFUS is efficient and less invasive, offering additional sphincter function assessment.

Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.

X-ray footprinting mass spectrometry (XFMS) is a structural biology method that uses broadband X-rays for hydroxyl radical labeling to map protein interactions and conformation in solution. However, while XFMS alone provides important structural information on biomolecules, as we move into the era of the interactome, hybrid methods are becoming increasingly necessary to gain a comprehensive understanding of protein complexes and interactions. Toward this end, we report the development of the first synergetic application of inline and real-time fluorescent spectroscopy at the Advanced Light Source's XFMS facility to study local protein interactions and global conformational changes simultaneously.