1x6y: Difference between revisions

Revision as of 03:06, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1x6y.png

Template:STRUCTURE 1x6y

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

Template:ABSTRACT PUBMED 15608379

About this StructureAbout this Structure

1X6Y is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 03:06:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structure 6: room temperature crystal structure of the truncated pak pilin from Pseudomonas aeruginosa at 1.80A resolution'''
+===Structure 6: room temperature crystal structure of the truncated pak pilin from Pseudomonas aeruginosa at 1.80A resolution===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15608379}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15608379 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15608379}}
 ==About this Structure==
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 [[Category: Lectin]]
 [[Category: Type iv pilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:38:50 2008''
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