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A comparative crystallographic analysis of earth-grown and space-grown crystals of AspRS-1, a large dimeric enzyme having flexible domains, shows that the latter are of enhanced quality. Their mosaicity as well as the electron-density map and the structure model derived from them are improved.

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The crystallization, cryoprotection and heavy-atom derivatization of insulin have been optimized using the counter-diffusion technique in a restricted geometry. The protein crystals obtained were immediately used for in situ X-ray diffraction, phase determination by SAS and electron-density map calculation without crystal manipulation.

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Aspartyl-tRNA synthetases were the model proteins in pilot crystallogenesis experiments. They are homodimeric enzymes of Mr~125 kDa that possess as substrates a transfer RNA, ATP and aspartate. They have been isolated from different sources and were crystallized either as free proteins or in association with their ligands. This review discusses their crystallisability with emphasis to crystal quality and structure determination. Crystallization in low diffusivity gelled media or in microgravity environments is highlighted. It has contributed to prepare high-resolution diffracting crystals with better internal order as reflected by their mosaicity. With AspRS from Thermus thermophilus, the better crystalline quality of the space-grown crystals within APCF is correlated with higher quality of the derived electron density maps. Usefulness for structural biology of targeted methods aimed to improve the intrinsic physical quality of protein crystals is highlighted.
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