| pubmed-article:21636924 | pubmed:abstractText | The binding between two universally conserved translation initiation factors, eIF5B and eIF1A, is important in the initiation step of eukaryotic protein synthesis on the ribosome. Through this interaction, eIF1A assists in recruiting eIF5B to the initiating 40S subunit; eIF5B then encourages the joining of the 60S subunit to form an initiating 80S ribosome. Here, the expression, purification, crystallization and preliminary X-ray analyses of eIF5B?N and the eIF5B?N-eIF1A?N complex from Saccharomyces cerevisiae are reported. The crystal of eIF5B?N diffracted to 2.45?Å resolution and belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 130.0, c = 71.7?Å. The asymmetric unit was estimated to contain one molecule. The initial phase was obtained by Se-SAD. The crystal of the eIF5B?N-eIF1A?N complex diffracted to 3.3?Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 101.9, b = 120.9, c = 132.8?Å. The asymmetric unit was estimated to contain two complex molecules. | lld:pubmed |
