2A7C

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

2A7C の概要

• エントリーDOI: 10.2210/pdb2a7c/pdb
• 分子名称: Elastase 1, SULFATE ION, XENON, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26344.53

構造登録者

Mueller-Dieckmann, C.,Panjikar, S.,Tucker, P.A.,Weiss, M.S. (登録日: 2005-07-05, 公開日: 2005-07-19, 最終更新日: 2024-11-06)

主引用文献

Mueller-Dieckmann, C.,Panjikar, S.,Tucker, P.A.,Weiss, M.S.
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength.
Acta Crystallogr.,Sect.D, 61:1263-1272, 2005

PubMed Abstract: Complete and highly redundant data sets were collected at different wavelengths between 0.80 and 2.65 A for a total of ten different protein and DNA model systems. The magnitude of the anomalous signal-to-noise ratio as assessed by the quotient R(anom)/R(r.i.m.) was found to be influenced by the data-collection wavelength and the nature of the anomalously scattering substructure. By utilizing simple empirical correlations, for instance between the estimated deltaF/F and the expected R(anom) or the data-collection wavelength and the expected R(r.i.m.), the wavelength at which the highest anomalous signal-to-noise ratio can be expected could be estimated even before the experiment. Almost independent of the nature of the anomalously scattering substructure and provided that no elemental X-ray absorption edge is nearby, this optimal wavelength is 2.1 A.

PubMed: 16131760
DOI: 10.1107/S0907444905021475

実験手法

X-RAY DIFFRACTION (1.65 Å)