1X6Q

Structure 3: cryocooled crystal structure of the truncated pak pilin from Pseudomonas aeruginosa at 1.51A resolution

Summary for 1X6Q

• Entry DOI: 10.2210/pdb1x6q/pdb
• Related: 1DZO
• Descriptor: Fimbrial protein (2 entities in total)
• Functional Keywords: type iv pilin, lectin, adhesin, structural protein
• Biological source: Pseudomonas aeruginosa
• Cellular location: Fimbrium: P02973
• Total number of polymer chains: 1
• Total formula weight: 12696.23

Authors

Dunlop, K.V.,Irvin, R.T.,Hazes, B. (deposition date: 2004-08-11, release date: 2005-04-19, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.51 Å)