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Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2

Item Type:Article
Title:Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2
Creators Name:Mueller, J.J. and Mueller, E.C. and Montag, T. and Zyto, N. and Loeschner, B. and Klein, H. and Heineman, U. and Otto, A.
Abstract:A novel lectin (SML-2) consisting of 138 amino acids was isolated from cyst merozoites of Sarcocystis muris and sequenced by Edman degradation and mass spectrometry. All 12 cysteinyl residues are involved in disulfide bridges, four of which are attributed to a characteristic pattern of cysteines as found in the so-called PAN-module superfamily. Crystals of SML-2 diffracting to 2.1 {angstrom} resolution at a synchrotron were grown by the hanging-drop vapour-diffusion technique. They belong to the space group P2 12 12 1, with unit-cell parameters a = 53.6, b = 128.8, c = 158.2 {angstrom} and eight molecules in the asymmetric unit. SML-2 cocrystallized with Au galactose results in two different crystal forms. The first form is isomorphous with the native crystals and the second form adopts space group C222 1, with unit-cell parameters a = 74.7, b = 82.0, c = 131.0 {angstrom}, and diffracts to 2.4 {angstrom} at a rotating-anode X-ray generator.
Keywords:Amino Acid Sequence, Amino Acid Sequence Homology, Crystallization, Electrospray Ionization Mass Spectrometry, Lectins, Molecular Sequence Data, Sarcocystis, X-Ray Crystallography, Animals
Source:Acta Crystallographica Section D
ISSN:0907-4449
Publisher:International Union of Crystallography (U.K.)
Volume:57
Number:7
Page Range:1042-1045
Date:1 January 2001
Official Publication:https://doi.org/10.1107/S0907444901007284
PubMed:View item in PubMed

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