1ame: Difference between revisions

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[[Category: freezing point]]
[[Category: freezing point]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:52:52 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:49:46 2007''

Revision as of 15:45, 30 October 2007

File:1ame.gif


1ame, resolution 1.65Å

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CRYSTAL STRUCTURE OF TYPE III ANTIFREEZE PROTEIN AT 4 C

OverviewOverview

Fish antifreeze proteins (AFP's) depress the freezing point of blood and, other body fluids below that of the surrounding seawater by binding to and, inhibiting the growth of seed ice crystals. The high-resolution crystal, structure of type III AFP, determined at room temperature, reveals a, remarkably flat surface containing most of the ice-binding residues [Jia, et al. (1996). Nature (London), 384, 285-288]. Since AFP's function at, temperatures close to 273 K, it is important to know whether the structure, determined at room temperature undergoes any change at much lower, temperature. Therefore, type III AFP has been crystallized at 277 K and, its structure determined. Although crystallization conditions at 277 K, were similar to those at approximately 295 K, crystal growth took much, ... [(full description)]

About this StructureAbout this Structure

1AME is a [Single protein] structure of sequence from [Macrozoarces americanus]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of type III antifreeze protein at 277 K., Ye Q, Leinala E, Jia Z, Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):700-2. PMID:9761880

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