Crystallization and preliminary X-ray crystallographic investigations on a betagamma-crystallin domain of absent in melanoma 1 (AIM1), a protein from Homo sapiens.
AIM1g1 is a single betagamma-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 A and were found to belong to space group P6(1) or P6(5), with unit-cell parameters a = b = 54.98, c = 59.73 A. Solvent-content analysis indicated the presence of one monomer per asymmetric unit.
Aravind
Penmatsa
P
Centre for Cellular and Molecular Biology, Hyderabad 500 007, India.
Rajini
Bheemreddy
B
Sharma
Yogendra
Y
Sankaranarayanan
Rajan
R
D003001:Cloning, Molecular; D003459:Crystallins; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D038204:beta-Crystallins / Q000737:chemistry; D038222:gamma-Crystallins / Q000737:chemistry
C105445:CRYBG1 protein, human; D003459:Crystallins; D008565:Membrane Proteins; D038204:beta-Crystallins; D038222:gamma-Crystallins