1X6P

Structure 4; room temperature crystal structure of truncated pak pilin from Pseudomonas aeruginosa at 1.63A resolution

1X6P の概要

• エントリーDOI: 10.2210/pdb1x6p/pdb
• 関連するPDBエントリー: 1DZO 1X6Q 1X6R 1X6X 1X6Y 1X6Z
• 分子名称: Fimbrial protein (2 entities in total)
• 機能のキーワード: type iv pilin, lectin, adhesin, structural protein
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Fimbrium: P02973
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12696.23

構造登録者

Dunlop, K.V.,Irvin, R.T.,Hazes, B. (登録日: 2004-08-11, 公開日: 2005-04-19, 最終更新日: 2024-10-30)

主引用文献

Dunlop, K.V.,Irvin, R.T.,Hazes, B.
Pros and cons of cryocrystallography: should we also collect a room-temperature data set?
Acta Crystallogr.,Sect.D, 61:80-87, 2005

PubMed Abstract: High-resolution protein structures are becoming more common owing to the availability of increasingly brilliant synchrotron X-ray sources. However, to withstand the increased X-ray dose the crystals must be held at cryogenic temperatures. To compare the benefit of increased resolution with the drawback of potential temperature-induced changes, three room-temperature and three cryogenic data sets for PAK pilin have been collected at resolutions between 1.8 and 0.78 A. The results show that although the high-resolution cryogenic structures are more precise and more detailed, they also show systematic deviations from the room-temperature structures. Small but significant differences are even observed in the structural core, whilst more extensive changes occur at the protein surface. These differences can affect biological interpretations, especially because many important biological processes take place at the protein surface. Accordingly, although high-quality cryogenic synchrotron data is extremely valuable to protein crystallography, room-temperature structures are still desirable, especially if the research question involves protein features that are sensitive to temperature-induced changes.

PubMed: 15608379
DOI: 10.1107/S0907444904027179

実験手法

X-RAY DIFFRACTION (1.63 Å)