3A39

Crystal Structure of High-Potential Iron-Sulfur Protein from Thermochromatium tepidum at 0.72 angstrom resolution

3A39 の概要

• エントリーDOI: 10.2210/pdb3a39/pdb
• 関連するPDBエントリー: 1EYT 1IUA 3A38
• 分子名称: High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: iron-sulfur cluster, electron transport
• 由来する生物種: Thermochromatium tepidum (Chromatium tepidum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9806.02

構造登録者

Takeda, K.,Kusumoto, K.,Hirano, Y.,Miki, K. (登録日: 2009-06-11, 公開日: 2009-10-27, 最終更新日: 2023-11-01)

主引用文献

Takeda, K.,Kusumoto, K.,Hirano, Y.,Miki, K.
Detailed assessment of X-ray induced structural perturbation in a crystalline state protein.
J.Struct.Biol., 169:135-144, 2010

PubMed Abstract: The positions of hydrogen atoms significantly define protein functions. However, such information from protein crystals is easily disturbed by X-rays. The damage can not be prevented completely even in the data collection at cryogenic temperatures. Therefore, the influence of X-rays should be precisely estimated in order to derive meaningful information from the crystallographic results. Diffraction data from a single crystal of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum were collected at an undulator beamline of a third generation synchrotron facility, and were merged into three data sets according to X-ray dose. A series of structures analyzed at 0.70A shows detailed views of the X-ray induced perturbation, such as the positional changes of hydrogen atoms of a water molecule. Based on the results, we successfully collected a low perturbation data set using attenuated X-rays. There was no influence on the crystallographic statistics, such as the relative B factors, during the course of data collection. The electron densities for hydrogen atoms were more clear despite the slightly lower resolution.

PubMed: 19782139
DOI: 10.1016/j.jsb.2009.09.012

実験手法

X-RAY DIFFRACTION (0.72 Å)