8DZ7

Hen lysozyme in orthorhombic space group at ambient temperature - diffuse scattering dataset

8DZ7 の概要

• エントリーDOI: 10.2210/pdb8dz7/pdb
• 分子名称: Lysozyme C, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: room temperature, diffuse scattering, lysozyme, hydrolase
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14389.60

構造登録者

Meisburger, S.P.,Imran, S.M.S.,Ando, N. (登録日: 2022-08-06, 公開日: 2022-09-07, 最終更新日: 2024-10-30)

主引用文献

Meisburger, S.P.,Case, D.A.,Ando, N.
Robust total X-ray scattering workflow to study correlated motion of proteins in crystals.
Nat Commun, 14:1228-1228, 2023

PubMed Abstract: The breathing motions of proteins are thought to play a critical role in function. However, current techniques to study key collective motions are limited to spectroscopy and computation. We present a high-resolution experimental approach based on the total scattering from protein crystals at room temperature (TS/RT-MX) that captures both structure and collective motions. To reveal the scattering signal from protein motions, we present a general workflow that enables robust subtraction of lattice disorder. The workflow introduces two methods: GOODVIBES, a detailed and refinable lattice disorder model based on the rigid-body vibrations of a crystalline elastic network; and DISCOBALL, an independent method of validation that estimates the displacement covariance between proteins in the lattice in real space. Here, we demonstrate the robustness of this workflow and further demonstrate how it can be interfaced with MD simulations towards obtaining high-resolution insight into functionally important protein motions.

PubMed: 36869043
DOI: 10.1038/s41467-023-36734-3

実験手法

X-RAY DIFFRACTION (1.34 Å)