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- W2015787672 abstract "Adenylosuccinate lyase (ASL) from Bacillus subtilis has been crystallized and structural analysis by X-ray diffraction is in progress. ASL is a 200-kDa homotetramer that catalyzes two distinct steps of de novo purine biosynthesis leading to the formation of AMP and IMP; both steps involve the β-elimination of fumarate. A single point mutation in the human ASL gene has been linked to mental retardation with autistic features. In addition, ASL plays an important role in the bioprocessing of anti-HIV therapeutics. B. subtilis ASL, which shares 30% sequence identity and 70% sequence similarity with human ASL, has been crystallized and data to 3.3 A have been collected at 100 K. The space group is P6122 or P6522 with a = b = 129.4 Å; the length of the c-axis varies between 275 and 290 Å, depending on the crystal. An analysis of solvent content indicates a dimer in the asymmetric unit, although a self-rotation function and an analysis of native Pattersons failed to identify unambiguously the location of any noncrystallographic symmetry axes. Structure determination by isomorphous replacement is in progress." @default.
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- W2015787672 title "Crystallization and preliminary structural analysis of<i>Bacillus subtilis</i>adenylosuccinate lyase, an enzyme implicated in infantile autism" @default.
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- W2015787672 doi "https://doi.org/10.1002/pro.5560050425" @default.
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