Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The first multi-bend achromat based synchrotron MAX IV operates two protein crystallography beamlines, BioMAX and MicroMAX. BioMAX is designed as a versatile, stable, high-throughput beamline catering for most protein crystallography experiments. MicroMAX is a more ambitious beamline dedicated to serial crystallography including time-resolved experiments. Both beamlines exploit the special characteristics of fourth-generation beamlines provided by the 3 GeV ring of MAX IV. In addition, the fragment-based drug discovery platform, FragMAX, is hosted and, at the FemtoMAX beamline, protein diffraction experiments exploring ultrafast time resolution can be performed. A technical and operational overview of the different beamlines and the platform is given as well as an outlook for protein crystallography embedded in the wider possibilities that MAX IV offers to users in the life sciences.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12067333 | PMC |
| http://dx.doi.org/10.1107/S1600577525002255 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Crystal structures of distinct parallel and antiparallel DNA G-quadruplexes reveal structural polymorphism in C9orf72 G4C2 repeats.
Nucleic Acids Res
September 2025
State Key Laboratory of Vaccines for Infectious Diseases, School of Public Health, Xiamen University, Xiamen 361102, Fujian, China.
The abnormal expansion of GGGGCC (G4C2) repeats in the noncoding region of the C9orf72 gene is a major genetic cause of two devastating neurodegenerative disorders, amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). These G4C2 repeats are known to form G-quadruplex (G4) structures, which are hypothesized to contribute to disease pathogenesis. Here, we demonstrated that four DNA G4C2 repeats can fold into two structurally distinct G4 conformations: a parallel and an antiparallel topology.
View Article and Find Full Text PDFStructural basis of adenosine 2A receptor-balanced signaling activation relies on allosterically mediated structural dynamics.
Cell Chem Biol
September 2025
iHuman Institute, ShanghaiTech University, Shanghai 201210, China; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China; Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA 92037, USA; Institute of Molecular Biology and Bio
Balanced or biased G protein and arrestin transmembrane signaling by the adenosine 2A receptor (AAR) is related to ligand-induced allosterically triggered variation of structural dynamics in the intracellular half of the transmembrane domain (TMD). F-nuclear magnetic resonance (NMR) of a network of genetically introduced meta-trifluoromethyl-L-phenylalanine (mtfF) probes in the core of the TMD revealed signaling-related structure rearrangements leading from the extracellular orthosteric drug-binding site to the G protein and arrestin contacts on the intracellular surface. The key element in this structural basis of signal transfer is dynamic loss of structural order in the intracellular half of the TMD, as manifested by local polymorphisms and associated rate processes within the molecular architecture determined previously by X-ray crystallography.
View Article and Find Full Text PDFStructural Insights into Fun174Sb from the GH174 Family Unravel Novel Subsite Specificities of the Endo-1,3-Fucanase.
J Agric Food Chem
September 2025
College of Food Science and Engineering, Ocean University of China, Qingdao 266404, PR China.
Sulfated fucan has attracted growing attention due to its diverse biological properties. Endo-1,3-fucanases are valuable tools for the degradation of sulfated fucan. This study characterized an endo-1,3-fucanase Fun174Sb from the GH174 family, utilizing a combination of protein crystallography, mutagenesis, computational biology, and nuclear magnetic resonance techniques.
View Article and Find Full Text PDFHuman sirtuin 2 (SIRT2) is an NAD dependant enzyme that has been linked to the pathogenesis of various diseases, making it a promising target for pharmaceutical intervention. This study presents a systematic investigation on the inhibitory effects of SIRT2 inhibitors functionalized with diverse electrophilic functional groups. Guided by initial docking studies, we designed and synthesised 14 derivatives of two published potent lead structures 24a and SirReal2.
View Article and Find Full Text PDFTemperature-Resolved Crystallography Reveals Rigid-Body Dominance over Local Flexibility in B‑Factors.
ACS Omega
September 2025
Laboratório de Biotecnologia Farmacêutica (pbiotech), Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
The crystallographic B-factor (Bf), also known as the Debye-Waller factor (DWF) or temperature factor, relates to the mean-square displacement of the atoms (X). X may be composed of individual contributions from lattice disorder (LT), static conformational heterogeneity (H) throughout the lattice, rigid body vibration (RB), local conformational vibration (V), and zero-point atomic fluctuation (A). The Bf has been widely employed as a surrogate measure of local protein flexibility, although such relation has not been confirmed.
View Article and Find Full Text PDF