The crystallization of biological macromolecules under microgravity: a way to more accurate three-dimensional structures?
The crystallization of proteins and other biological particles (including nucleic acids, nucleo-protein complexes and large assemblies such as nucleosomes, ribosomal subunits or viruses) in a microgravity environment can produce crystals having lesser defects than crystals prepared under normal gravity on earth. Such microgravity-grown crystals can diffract X-rays to a higher resolution and have a lower mosaic spread. The inferred electron density maps can be richer in details owing to which more accurate three-dimensional structure models can be built. Major results reported in this field of research are reviewed. Novel ones obtained with the Advanced Protein Crystallization Facility are presented. For structural biology, practical applications and implications associated with crystallization and crystallography onboard the International Space Station are discussed.
Lorber
Bernard
B
Département Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogénèse' UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 rue René Descartes, F-67084 Strasbourg, France. B.Lorber@ibmc.u-strasbg.fr
D000818:Animals; D003460:Crystallization; D006801:Humans; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014893:Weightlessness
D011506:Proteins