The fabrication and testing of a prototype deep-depletion direct-conversion X-ray CCD detector are described. The device is fabricated on 600 µm-thick high-resistivity silicon, with 24 × 24 µm pixels in a 4k × 4k pixel format. Calibration measurements and the results of initial protein crystallography experiments at the Cornell High Energy Synchrotron Source (CHESS) F1 beamline are described, as well as suggested improvements for future versions of the detector.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3769057PMC
http://dx.doi.org/10.1107/S0021889813016592DOI Listing

Publication Analysis

Top Keywords

protein crystallography
8
prototype direct-detection
4
direct-detection ccd
4
ccd protein
4
crystallography fabrication
4
fabrication testing
4
testing prototype
4
prototype deep-depletion
4
deep-depletion direct-conversion
4
direct-conversion x-ray
4

Similar Publications

Loss of Bcl2-associated athanogene 3 (BAG3) is associated with dilated cardiomyopathy (DCM). BAG3 regulates sarcomere protein turnover in cardiomyocytes; however, the function of BAG3 in other cardiac cell types is understudied. In this study, we used an isogenic pair of BAG3-knockout and wild-type human induced pluripotent stem cells (hiPSCs) to interrogate the role of BAG3 in hiPSC-derived cardiac fibroblasts (CFs).

View Article and Find Full Text PDF

Leveraging Cryptic Ligand Envelopes through Enhanced Molecular Simulations.

J Phys Chem Lett

December 2024

Molecular Ocean Lab, Institute for Advanced Chemistry of Catalonia, IQAC-CSIC, Carrer de Jordi Girona 18-26, 08034 Barcelona, Spain.

Protein-bound ligands can adopt a range of different conformations, collectively defining a ligand envelope that has proven to be crucial for the design of potent and selective drugs. Yet, the cryptic nature of this ligand envelope makes it difficult to visualize, characterize, and ultimately exploit for drug design. Using enhanced molecular dynamics simulations, here, we provide a general framework to reconstruct the cryptic ligand envelope that is dynamically accessible by protein-bound small molecules in solution.

View Article and Find Full Text PDF

Invasive fungal infections are a leading cause of death worldwide. Translating molecular insights into clinical benefits is challenging because fungal pathogens and their hosts share similar eukaryotic physiology. Consequently, current antifungal treatments have limited efficacy, may be poorly fungicidal in the host, can exhibit toxicity, and are increasingly compromised by emerging resistance.

View Article and Find Full Text PDF

Molecular basis of hemoglobin binding and heme removal in .

Proc Natl Acad Sci U S A

January 2025

Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095.

To successfully mount infections, nearly all bacterial pathogens must acquire iron, a key metal cofactor that primarily resides within human hemoglobin. causes the life-threatening respiratory disease diphtheria and captures hemoglobin for iron scavenging using the surface-displayed receptor HbpA. Here, we show using X-ray crystallography, NMR, and in situ binding measurements that selectively captures iron-loaded hemoglobin by partially ensconcing the heme molecules of its α subunits.

View Article and Find Full Text PDF

Reversible protein phosphorylation directs essential cellular processes including cell division, cell growth, cell death, inflammation, and differentiation. Because protein phosphorylation drives diverse diseases, kinases and phosphatases have been targets for drug discovery, with some achieving remarkable clinical success. Most protein kinases are activated by phosphorylation of their activation loops, which shifts the conformational equilibrium of the kinase toward the active state.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!