Open AccessCrystallization and preliminary X‐ray crystallographic investigations on a βγ‐crystallin domain of absent in melanoma 1 (AIM1), a protein from Homo sapiens
Author(s) -
Aravind Penmatsa,
Rajini Bheemreddy,
Sharma Yogendra,
Sankaranarayanan Rajan
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106005380
Subject(s) - crystallization , crystallography , monomer , resolution (logic) , crystallin , domain (mathematical analysis) , chemistry , solvent , biology , biophysics , materials science , biochemistry , polymer , computer science , mathematical analysis , mathematics , organic chemistry , artificial intelligence
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 P 6 1 or P 6 5 , with unit‐cell parameters a = b = 54.98, c = 59.73 Å. Solvent‐content analysis indicated the presence of one monomer per asymmetric unit.