8P2Q

Crystal structure of Hen Egg White Lysozyme co-crystallized with 10 mM TbXo4-OH

Summary for 8P2Q

• Entry DOI: 10.2210/pdb8p2q/pdb
• Related: 8OWC
• Descriptor: Lysozyme C, TbXo4-OH, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: hewl, crystallophore variants, nucleating agent, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 17072.35

Authors

Alsalman, Z.,Girard, E. (deposition date: 2023-05-16, release date: 2024-06-05, Last modification date: 2024-11-20)

Primary citation

Roux, A.,Alsalman, Z.,Jiang, T.,Mulatier, J.C.,Pitrat, D.,Dumont, E.,Riobe, F.,Gillet, N.,Girard, E.,Maury, O.
Influence of Chemical Modifications of the Crystallophore on Protein Nucleating Properties and Supramolecular Interactions Network.
Chemistry, 30:e202400900-e202400900, 2024

PubMed Abstract: Crystallophores are lanthanide complexes that have demonstrated outstanding induction of crystallization for various proteins. This article explores the effect of tailored modifications of the crystallophore first generation and their impact on the nucleating properties and protein crystal structures. Through high-throughput crystallization experiments and dataset analysis, we evaluated the effectiveness of these variants, in comparison to the first crystallophore generation G. In particular, the V variant, featuring a propanol pendant arm, demonstrated the ability to produce new crystallization conditions for the proteins tested (hen-egg white lysozyme, proteinase K and thaumatin). Structural analysis performed in the case of hen egg-white lysozyme along with Molecular Dynamics simulations, highlights V's unique behavior, taking advantage of the flexibility of its propanol arm to explore different protein surfaces and form versatile supramolecular interactions.

PubMed: 38738452
DOI: 10.1002/chem.202400900

Experimental method

X-RAY DIFFRACTION (1.69 Å)