Improvements in Thermostable T1 lipase protein crystal through microgravity growth (#213)
Three-dimensional structure of thermostable lipase is much sought after nowadays as it is important for industrial application. High resolution protein crystal data is important in revealing a highly accurate structure at atomic level. Thermostable T1 lipase enzyme has been crystallized in laboratory on earth and also under microgravity condition aboard Progress spacecraft to the ISS in collaboration with JAXA (Japanese Aerospace Exploration Agency). This study is conducted with the aims of improving crystal packing and structure resolution. A new form of well-ordered high quality three dimensional crystal of T1 lipase has been obtained via counter diffusion method in space. The diffraction data set for space grown crystal was collected to 1.1 Å resolution and 1.3 Å resolution for ground grown crystal. Both are belonged to monoclinic C2 Space group. Comparative crystallographic analysis revealed that the space-grown crystal was better than ground-grown crystal. It shows that the crystals grown in space are highly improved. Analysis of data collection and refinement statistics showed that crystallization in counter diffusion method using microgravity environment improved the internal order of crystals thus gave a more precise three dimensional structure.