2G4K

Anomalous substructure of human ADP-ribosylhydrolase 3

2G4K の概要

• エントリーDOI: 10.2210/pdb2g4k/pdb
• 関連するPDBエントリー: 2G4H 2G4I 2G4J 2G4L 2G4M 2G4N 2G4O 2G4P 2G4Q 2G4R 2G4S 2G4T 2G4U 2G4V 2G4W 2G4X 2G4Y 2G4Z 2G51 2G52 2G55
• 分子名称: ADP-ribosylhydrolase 3, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: adp-ribosylhydrolase 3, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37963.91

構造登録者

Mueller-Dieckmann, C.,Weiss, M.S. (登録日: 2006-02-22, 公開日: 2007-02-20, 最終更新日: 2024-02-14)

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 (1.82 Å)