Crystallization and preliminary X-ray crystallographic investigations on a βγ-crystallin domain of absent in melanoma 1 (AIM1), a protein from Homo sapiens
- Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007 (India)
The crystallization and preliminary X-ray diffraction analysis of AIM1g1, a βγ-crystallin domain of absent in melanoma (AIM1) protein from H. sapiens, is reported. 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 P6{sub 1} or P6{sub 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.
- OSTI ID:
- 22356287
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 3; Other Information: PMCID: PMC2197174; PMID: 16511323; PUBLISHER-ID: en5157; OAI: oai:pubmedcentral.nih.gov:2197174; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
Crystallization and preliminary X-ray diffraction studies of the ISC-like [2Fe–2S] ferredoxin (FdxB) from Pseudomonas putida JCM 20004