4LR3

Crystal structure of E. coli YfbU at 2.5 A resolution

4LR3 の概要

• エントリーDOI: 10.2210/pdb4lr3/pdb
• 分子名称: protein YfbU, MAGNESIUM ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: helical tetramer, apoptosis
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 315925.50

構造登録者

Wang, J.,Wing, R.A. (登録日: 2013-07-19, 公開日: 2014-04-30, 最終更新日: 2024-02-28)

主引用文献

Wang, J.,Wing, R.A.
Diamonds in the rough: a strong case for the inclusion of weak-intensity X-ray diffraction data.
Acta Crystallogr.,Sect.D, 70:1491-1497, 2014

PubMed Abstract: Overwhelming evidence exists to show that the inclusion of weak-intensity, high-resolution X-ray diffraction data helps improve the refinement of atomic models by imposing strong constraints on individual and overall temperature B factors and thus the quality of crystal structures. Some researchers consider these data to be of little value and opt to discard them during data processing, particularly at medium and low resolution, at which individual B factors of atomic models cannot be refined. Here, new evidence is provided to show that the inclusion of these data helps to improve the quality of experimental phases by imposing proper constraints on electron-density models during noncrystallographic symmetry (NCS) averaging. Using electron-density correlation coefficients as criteria, the resolution of data has successfully been extended from 3.1 to 2.5 Å resolution with redundancy-independent merging R factors from below 100% to about 310%. It is further demonstrated that phase information can be fully extracted from observed amplitudes through de novo NCS averaging. Averaging starts with uniform density inside double-shelled spherical masks and NCS matrices that are derived from bound heavy-atom clusters at the vertices of cuboctahedrally symmetric protein particles.

PubMed: 24816117
DOI: 10.1107/S1399004714005318

実験手法

X-RAY DIFFRACTION (2.5 Å)