F Immunological Societies (IUIS). Soybean proteins are composed of two key components: -conglycinin (7S globulin) and glycinin (11S globulin). -Conglycinin is composed of ( 67 kDa), 0 ( 71 kDa) and ( 50 kDa) subunits, whereas glycinin is composed of five subunits (Staswick et al., 1984) divided into group I [A1aB1b (53.6 kDa), A1bB2 (52.2 kDa) and A2B1a (52.4 kDa)] and group II [A3B4 (55.4 kDa) and A5A4B3 (61.two kDa)]. In establishing seeds, the glycinins are synthesized as a single polypeptide precursor within the rough endoplasmic reticulum, where the co-translational signal peptide cleavage and subsequent trimer (proglycinin) assembly happen. The proteins are then transported and cleaved into an acidic ( 30 kDa) plus a simple ( 20 kDa) polypeptide (except for A4 of A5A4B3) by a vacuolar processing enzyme within the protein-storage vacuole. The polypeptides are linked by a disulfide bond and also the mature proteins assemble into hexamers (Dickinson et al., 1989). The hexamers of glycinin are formed by random subunit combination. The proteins play distinct roles in food and non-food soybean protein goods owing to their distinct physicochemical properties for instance hydrophobicity, solubility, thermal stability and emulsification (Utsumi, 1992; Utsumi et al., 1997). These properties are specially distinct among groups I and II of glycinin (Maruyama et al., 2004; Prak et al., 2005). A big quantity of European and Japanese soybean-allergenic individuals have IgE antibodies to glycinin and -conglycinin (Holzhauser et al., 2009;doi:ten.1107/SKrisna Prak,a,b Bunzo Mikami,c Takafumi Itoh,c,d Takako Fukuda,a Nobuyuki Maruyamaa* and Shigeru UtsumiaaLaboratory of Meals Quality Design and Development, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan, bLaboratory for Molecular Cell Biology, Healthcare Study Council, University College London, London WC1E 6BT, England, cLaboratory of Applied Structural Biology, Division of Applied Life Sciences, Graduate College of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan, and dDivision of Applied Biochemistry and Biomolecular Engineering, Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka Kenjyoujima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, JapanDeceased on 1 December 2008.7-Bromochromane-3-carboxylic acid Chemscene Correspondence e-mail: marunobu@kais.tert-Butyl 9-bromononanoate structure kyoto-u.ac.jpReceived 5 June 2013 Accepted 16 JulyActa Cryst. (2013). F69, 937?crystallization communicationsIto et al., 2011). The structural evaluation of these proteins is crucial for the improvement on the nutritional qualities and functional properties of these proteins, at the same time as for elucidation of their allergenicity (Prak et al.PMID:23746961 , 2006, 2007; Prak Utsumi, 2009; Tandang et al., 2005). Having said that, as a result of the heterogeneity of your molecular species, it truly is tough to crystallize mature glycinin ready from normal soybean cultivars (Utsumi, 1992). Applying the Escherichia coli expression method, we are able to only get 11S globulin in the kind of proglycinin. To receive the mature glycinin structure, we need to prepare the protein from a mutant soybean cultivar; we hence successfully elucidated the structure in the glycinin A3B4 homohexamer (Adachi et al., 2003). Within this study, we report the isolation, purification and crystallization of the A1bB2 mature glycinin subunit from a mutant soybean cultivar, also as the X-ray diffraction outcomes obtained. buffer B was mixed with 1 ml reservoir solution. Crystallization was performed at 281.