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L. Stirling, K. Willcox, P. Ferguson, D. Newman (2009)
Kinetics and kinematics for translational motions in microgravity during parabolic flight.Aviation, space, and environmental medicine, 80 6
W. Shenton, S. Mann, H. Cölfen, A. Bacher, M. Fischer (2001)
Synthesis of Nanophase Iron Oxide in Lumazine Synthase Capsids.Angewandte Chemie, 40 2
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The atomic structure of pentameric lumazine synthase from Saccharomyces cerevisiae at 1.85 A resolution reveals the binding mode of a phosphonate intermediate analogue.Journal of molecular biology, 299 1
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Icosahedral macromolecules have a wide spectrum of potential nanotechnological applications, the success of which relies on the level of accuracy at which the molecular structure is known. Lumazine synthase from Bacillus subtilis forms a 150 Å icosahedral capsid consisting of 60 subunits and crystallizes in space group P6322 or C2. However, the quality of these crystals is poor and structural information is only available at 2.4 Å resolution. As classical strategies for growing better diffracting crystals have so far failed, protein engineering has been employed in order to improve the overexpression and purification of the molecule as well as to obtain new crystal forms. Two cysteines were replaced to bypass misfolding problems and a charged surface residue was replaced to force different molecular packings. The mutant protein crystallizes in space group R3, with unit‐cell parameters a = b = 313.02, c = 365.77 Å, α = β = 90.0, γ = 120°, and diffracts to 1.6 Å resolution.
Acta Crystallographica Section F – Wiley
Published: Jul 1, 2008
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