Crystallization and preliminary X-ray studies of sialidase L from the leech Macrobdella decora.
Functional monomeric 83 kDa sialidase L, a NeuAcalpha2-->3Gal-specific sialidase from Macrobdella leech, was expressed in Escherichia coli and readily crystallized by a macroseeding technique. The crystal belongs to space group P1 with unit-cell parameters a = 46.4, b = 69.3, c = 72.5 A, alpha = 113.5, beta = 95.4 and gamma = 107.3 degrees. There is one molecule per unit cell, giving a Vm = 2.4 A3 Da-1 and a solvent content of 40%. Native and mercury-derivative data sets were collected to 2.0 A resolution. Threading and molecular-replacement calculations confirmed the existence of a bacterial sialidase-like domain.
Center for Macromolecular Crystallography, University of Alabama at Birmingham, Alabama 35294, USA.
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Luo
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Chou
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Li
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Luo
D000818:Animals; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D005583:Fourier Analysis; D007865:Leeches / Q000201:enzymology*; D009439:Neuraminidase / Q000737:chemistry*
C100877:sialidase L; D009439:Neuraminidase