KAUST researchers used cryogenic electron microscopy (cryo-EM) to study the 3D structure of protein complexes involved in DNA replication and repair. They investigated the interaction between the Y-family TLS polymerase Pol K and mono-ubiquitylated PCNA. The study revealed that DNA binding is required for Pol K to form a rigid, active complex with PCNA. Why it matters: Understanding these structural interactions may provide insights into cancer development and drug resistance mechanisms.
KAUST researchers developed a new methodology for high-resolution transmission electron microscopy (TEM) imaging of beam-sensitive materials. The method addresses challenges in acquiring images with low electron doses, aligning images, and determining defocus values. The processes incorporate two provisional patents and are applicable to aligning nanosized crystals and noisy images with periodic features. Why it matters: This advancement enables the study of delicate materials like MOFs at atomic resolution, with broad applications in materials science and nanotechnology.
KAUST researchers have captured the initial unwinding of DNA using cryo-electron microscopy and deep learning. The study details 15 atomic states describing how the Simian Virus 40 Large Tumor Antigen helicase unwinds DNA, revealing the coordinated roles of DNA, helicases, and ATP. The research elucidates the fundamental mechanisms of DNA replication, a cornerstone of growth and reproduction. Why it matters: This detailed understanding of helicase function could lead to advances in nanotechnology and our understanding of genetic processes.
KAUST and Thermo Fisher Scientific launched an Electron Microscopy Center of Excellence on May 9. The Center expands the existing partnership between KAUST and Thermo Fisher, focusing on instrument performance and R&D collaboration. It features the FEI Titan Themis Z scanning transmission electron microscope, the first installation globally. Why it matters: The center will provide advanced materials science research capabilities to KAUST researchers, industry partners, and Saudi Arabia, enhancing scientific discovery and technological advancement in the region.
KAUST researchers have determined the atomic 3D structure of a key protein involved in plant stress signaling using X-ray crystallography at the SOLEIL synchrotron in France. Postdoctoral fellow Umar Farook Shahul Hameed optimized a tiny crystal of the plant enzyme for over six months. The team used the EIGER 9M detector to capture the weak diffraction pattern from the crystal. Why it matters: Understanding the interactions between proteins that communicate plant stress could lead to engineering more stress-tolerant crops, enhancing food security.
KAUST hosted the Electron Microscopy Frontiers conference from December 9-11, marking five years of electron microscopy activities at the university. The symposium featured over 20 speakers from international universities and research institutions. It aimed to foster scientific collaborations and showcase KAUST's growing role as a leading electron microscopy laboratory in the Middle East. Why it matters: The conference signals KAUST's ambition to become a hub for advanced microscopy research and collaboration in the region, potentially driving innovation in materials science and bioscience.
KAUST Discovery Associate Professor Stefan Arold has established KAUST's first structural biology lab specializing in determining the atomic 3D structure of proteins and other biological macromolecules. The lab setup involved challenges such as assembling instruments and continuing research, but the Bioscience Core Lab at KAUST and support from colleagues aided in the process. Arold's research focuses on understanding protein function through an integrated 'hybrid' approach to analyze 3D structure and function of proteins. Why it matters: This new lab enhances KAUST's capabilities in molecular biophysics and structural biology, enabling advanced research into the functions of proteins and their implications for health and disease.
Daisuke Kihara from Purdue University presented a seminar at MBZUAI on using deep learning for biomolecular structure modeling. His lab is developing 3D structure modeling methods, especially for cryo-electron microscopy (cryo-EM) data. They are also working on RNA structure prediction and peptide docking using deep neural networks inspired by AlphaFold2. Why it matters: Applying advanced deep learning techniques to biomolecular structure prediction can accelerate drug discovery and our understanding of molecular functions.