Crystallization and preliminary X-ray crystallographic investigations on a βγ-crystallin domain of absent In melanoma 1 (AIM1), a protein from Homo sapiens

Aravind, P. ; Rajini, B. ; Sharma, Y. ; Sankaranarayanan, R. (2006) Crystallization and preliminary X-ray crystallographic investigations on a βγ-crystallin domain of absent In melanoma 1 (AIM1), a protein from Homo sapiens Acta Crystallographica Section F, 62 . pp. 282-284. ISSN 1744-3091

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Official URL: http://scripts.iucr.org/cgi-bin/paper?en5157

Related URL: http://dx.doi.org/10.1107/S1744309106005380

Abstract

AIM1g1 is a single βγ-crystallin domain from the protein absent in melanoma 1 (AIM1), which appears to play a role in the suppression of melanomas. This domain is known to bind calcium and its structure would help in identifying calcium-coordinating sites in vertebrate crystallins, which have hitherto been believed to have lost this ability during evolution. Crystallization of this domain was performed by the hanging-drop vapour-diffusion method. Crystals diffracted to a maximum resolution of 1.86 Å and were found to belong to space group P61 or P65, with unit-cell parameters a = b = 54.98, c = 59.73 Å. Solvent-content analysis indicated the presence of one monomer per asymmetric unit.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:AIM1g1; βγ-crystallin; Calcium; Greek-key Motif
ID Code:66854
Deposited On:28 Oct 2011 04:02
Last Modified:16 Nov 2011 12:40

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