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Low-resolution ab initio phasing of Sarcocystis muris lectin SML-2

Item Type:Article
Title:Low-resolution ab initio phasing of Sarcocystis muris lectin SML-2
Creators Name:Mueller, J.J. and Lunina, N.L. and Urzhumtsev, A. and Weckert, E. and Heinemann, U. and Lunin, V.Y.
Abstract:Structural analysis of the lectin SML-2 faced difficulties when applying standard crystallographic phasing methods. The connectivity-based ab initio phasing method allowed the computation of a 16 A resolution Fourier synthesis and the derivation of primary structural information. It was found that SML-2 crystals have three dimers in the asymmetric part of the unit cell linked by a noncrystallographic symmetry close to translation by (0, 0, 1/3). A clear identification of the noncrystallographic twofold axis explains the space-group transformation from the primitive P2(1)2(1)2(1) to the C-centred C222(1) observed during annealing procedures within an N(2) cryostream for cocrystals of SML-2 and galactose. Related packing considerations predict a possible arrangement of SML-2 molecules in a tetragonal unit cell. Multiple noncrystallographic symmetries and crystal forms provide a basis for further image improvements.
Keywords:Ab Initio Phasing, Lectins, SML-2, Animals
Source:Acta Crystallographica Section D
Publisher:International Union of Crystallography
Number:Pt 5
Page Range:533-540
Date:May 2006
Official Publication:https://doi.org/10.1107/S0907444906007591
PubMed:View item in PubMed

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