2ILL

Anomalous substructure of Titin-A168169

2ILL の概要

• エントリーDOI: 10.2210/pdb2ill/pdb
• 分子名称: Titin, CHLORIDE ION (3 entities in total)
• 機能のキーワード: long wavelength, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (Probable): Q8WZ42
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21708.60

構造登録者

Mueller-Dieckmann, C.,Weiss, M.S. (登録日: 2006-10-03, 公開日: 2007-02-20, 最終更新日: 2024-03-13)

主引用文献

Mueller-Dieckmann, C.,Panjikar, S.,Schmidt, A.,Mueller, S.,Kuper, J.,Geerlof, A.,Wilmanns, M.,Singh, R.K.,Tucker, P.A.,Weiss, M.S.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths
ACTA CRYSTALLOGR.,SECT.D, 63:366-380, 2007

PubMed Abstract: 23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.

PubMed: 17327674
DOI: 10.1107/S0907444906055624

実験手法

X-RAY DIFFRACTION (2.2 Å)