NORMAL GENOMIC

• Shi Z et al.
• Expression, purification, crystallization and preliminary X-raycrystallographic analysis of the SH3 domain of human AHI1.
• Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009; 65: 361-3
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• The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli.The protein was purified by affinity and size-exclusion chromatography andwas crystallized using the sitting-drop vapour-diffusion method at 293 K.A complete data set was collected to 2.5 A resolution at 110 K. Thecrystal belonged to space group P4(1)2(1)2, with unit-cell parameters a =67.377, b = 67.377, c = 98.549 A.

• Lin L et al.
• Crystallization and preliminary X-ray crystallographic analysis of aconserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3.
• Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005; 61: 414-6
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• A plant- and prokaryote-conserved domain (PPC) has previously been foundin AT-hook motif nuclear localized protein 1 (AHL1) localized in thenuclear matrix of Arabidopsis thaliana (AtAHL1). AtAHL1 has a DNA-bindingfunction. Mutation analyses of AtAHL1 has previously revealed that thehydrophobic region of the PPC domain is essential for its nuclearlocalization. In this study, the PPC of the hyperthermophilicarchaebacterium Pyrococcus horikoshii (PhPPC) was crystallized using thehanging-drop vapour-diffusion method. The crystals belonged to thehexagonal space group P6(3)22, with unit-cell parameters a = b = 53.69, c= 159.2 A. Data were obtained at 100 K, with diffraction being observed toa resolution of 1.7 A. A complete data set from crystals of theSeMet-substituted protein was also obtained.

• Leech A, Mattei B, Federici L, De Lorenzo G, Hemmings AM
• Preliminary X-ray crystallographic analysis of a plant defence protein,the polygalacturonase-inhibiting protein from Phaseolus vulgaris.
• Acta Crystallogr D Biol Crystallogr. 2000; 56: 98-100
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• A leucine-rich repeat plant protein involved in resistance to pathogens, apolygalacturonase-inhibiting protein (PGIP-1) from Phaseolus vulgaris, hasbeen crystallized and preliminary X-ray characterization has beenperformed. The protein contains ten repeats of a short (24 amino-acid)leucine-rich repeat motif. Single crystals of the protein were grown fromvapour-diffusion experiments using PEG 2K monomethylether as precipitant;these crystals diffract to at least 2.3 A resolution. The space group isP2(1), with two molecules of PGIP-1 in the asymmetric unit; the crystalscontain approximately 38% solvent.

• Rao KN, Gurjar MM, Gaikwad SM, Khan MI, Suresh CG
• Crystallization and preliminary X-ray studies of the basic lectin from theseeds of Artocarpus hirsuta.
• Acta Crystallogr D Biol Crystallogr. 1999; 55: 1204-5
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• The basic lectin from Artocarpus hirsuta specific towards methylalpha-galactose has been purified and crystallized using the hanging-dropvapour-diffusion method with ammonium sulfate as precipitant. Threedifferent crystal forms, orthorhombic I, orthorhombic II and hexagonal,were grown under the same crystallization conditions. The orthorhombicforms belonged to space group P212121 with unit-cell dimensions a = 92.9,b = 99.8, c = 166. 2 A and a = 89.9, b = 121.9, c = 131.6 A, respectively.The unit-cell dimensions of the hexagonal form were a = b = 84.1 and c =271.7 A and the space group was P6122.

• Esaka M, Hayakawa H
• Specific secretion of proline-rich proteins by salt-adapted winged beancells.
• Plant Cell Physiol. 1995; 36: 441-6
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• Six proteins, designated SAP1 through SAP6, were secreted specifically bysalt-adapted cells of winged bean (Psophocarpus tetragonolobus) insuspension cultures. The amino-terminal amino acid sequences of SAP2 (57kDa), SAP4 (21 kDa), SAP5 (19 kDa) and SAP6 (17 kDa) were homologous tothe sequences of proline-rich proteins, indicating that proline-richproteins are secreted specifically by these salt-adapted cells. Inaddition, the amino-terminal amino acid sequence of SAP2 was identical tothat of SAP4, and the amino-terminal sequence of SAP5 was identical tothat of SAP6. Secretion of SAP2 was significantly enhanced by addition ofAlCl3 but not of KCl, LiCl, CaCl2, MgCl2, mannitol or sucrose tosuspension cultures. Furthermore, secretion of SAP4, SAP5 and SAP6 wasstimulated by addition of abscisic acid to cultures, suggesting that theseproteins might be secreted in response to salt or osmotic stress.

• Shet MS, Madaiah M
• Chemical modification studies on a lectin from winged-bean [Psophocarpustetragonolobus (L.) DC] tubers.
• Biochem J. 1988; 254: 351-7
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• The effect of chemical modification on a D(+)-galactose-specific lectinisolated from winged-bean tubers was investigated to identify the type ofamino acid involved in its haemagglutinating activity. Various anhydridesof dicarboxylic acids, such as acetic anhydride, succinic anhydride,maleic anhydride and citraconic anhydride, modified 57-68% of the aminogroups of the winged-bean tuber lectin. Treatment with N-acetylimidazolemodified only 45% of the total amino groups. Reductive methylation of freeamino groups modified 57% of the amino groups. Modification of the aminogroups of the lectin by acetic anhydride and succinic anhydride did notlead to any significant change in the haemagglutinating activity (greaterthan or equal to 75% active). However, citraconylation and maleylation ofthe lectin led to a significant decrease in the haemagglutinating activity(less than or equal to 20% active). Acetylation and succinylation(3-carboxypropionylation) of the lectin led to a decrease in the pI valueof the native lectin from approx. 9.5 to approx. 4.5. Treatment of thelectin with N-bromosuccinimide led to the modification of two and fourtryptophan residues per molecule in the absence and in the presence of 8M-urea respectively. The immunological identity of all the modified lectinpreparations showed no gross structural changes except the lectin modifiedwith N-bromosuccinimide in the presence of urea at pH 4.0.