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Structure 6: room temperature crystal structure of the truncated pak pilin from Pseudomonas aeruginosa at 1.80A resolutionStructure 6: room temperature crystal structure of the truncated pak pilin from Pseudomonas aeruginosa at 1.80A resolution
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHigh-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. Pros and cons of cryocrystallography: should we also collect a room-temperature data set?,Dunlop KV, Irvin RT, Hazes B Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):80-7. Epub 2004 Dec, 17. PMID:15608379[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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