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Ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer is a good model for the study of the thermostability of proteins. It has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method using PEG 8000 as precipitant at 290 K. The crystal belongs to the hexagonal space group P61/P65, with unit-cell parameters a = b = 48.32, c = 86.42 Å. The asymmetric unit contains a single molecule of L30e, with a corresponding crystal volume per protein mass (VM) of 2.68 Å3 Da−1 and a solvent content of 54%. A complete data set diffracting to 1.96 Å resolution was collected from a single crystal at 100 K.

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