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  • 1
    Digitale Medien
    Digitale Medien
    Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 779-784 
    Details
    ISSN: 1399-0047
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: Enzymatic and non-enzymatic iodination of the amino acid tyrosine is a well known phenomenon. The iodination technique has been widely used for labeling proteins. Using high-resolution X-ray crystallographic techniques, the chemical and three-dimensional structures of iodotyrosines formed by non-enzymatic incorporation of I atoms into tyrosine residues of a crystalline protein are described. Acetylxylan esterase (AXE II; 207 amino-acid residues) from Penicillium purpurogenum has substrate specificities towards acetate esters of D-xylopyranose residues in xylan and belongs to a new class of α/β hydrolases. The crystals of the enzyme are highly ordered, tightly packed and diffract to better than sub-ångström resolution at 85 K. The iodination technique has been utilized to prepare an isomorphous derivative of the AXE II crystal. The structure of the enzyme determined at 1.10 Å resolution exclusively by normal and anomalous scattering from I atoms, along with the structure of the iodinated complex at 1.80 Å resolution, demonstrate the formation of covalent bonds between I atoms and C atoms at ortho positions to the hydroxyl groups of two tyrosyl moieties, yielding iodotyrosines.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0907444999000244
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  • 2
    Digitale Medien
    Digitale Medien
    Crystal and molecular structure of aN(2)-benzyl-1,3-disubstituted-1,2,3,4-tetrahydro-β-carboline (1990)
    Springer
    Journal of chemical crystallography 20 (1990), S. 109-115 
    Details
    ISSN: 1572-8854
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Geologie und Paläontologie , Physik
    Notizen: Abstract (1R,3S)-2-Benzyl-3-methoxycarbonyl-1-methylcarboxymethyl-1,2,3,4-tetrahydro-9H-pyrido [3,4-b] indole, C23H24N2O4, was synthesized by a modified Pictet-Spengler reaction, and its crystal and molecular structure determined by single crystal X-ray diffraction methods. The crystals are monoclinic:P21 (No. 4),a=11.336(1),b=8.919(1),c=10.314(1)Å,β=100.81(1)°,Z=2. The structure has been solved by direct methods, and refined toR=0.041 for 2203 observed reflections. The six-membered heterocyclic ring is in a half-chair conformation, and the substituents at C(3) and C(5) occupy axial and equatorial positions respectively. The CH2Ph group attached to N(4) is in the generally less favoured axial position. The nitrogen atom of the indole system forms an intermolecular hydrogen bond with the carbonyl oxygen of the CH2CO2 Me group, the N⋯O distance being 2.995(3)Å.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01160961
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  • 3
    Digitale Medien
    Digitale Medien
    Purification and crystallization of insecticidal δ-endotoxin CryIIIB2 from Bacillus thuringiensis (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 14 (1992), S. 324-324 
    Details
    ISSN: 0887-3585
    Schlagwort(e): Bacillus thuringiensis ; insecticidal ; δ-endotoxin ; crystallization ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: CryIIIB2, an insecticidal protein from Bacillus thuringiensis has been crystallized from 0.6 M NaBr and HEPES buffer at pH 7.0 and X-ray diffraction data collected on a native crystal to 2.4 Å. The insecticidal protein was obtained from a Bacillus thuringiensis (Bt) strain EG7231. Crystals of the endotoxin are orthorhombic, space group C2221, with unit cell dimensions of a = 122.44, b = and c = Å. A unit cell contains one molecule of the 67,000 Da endotoxin per asymmetric unit. © 1992 Wiley-Liss, Inc.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340140217
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  • 4
    Digitale Medien
    Digitale Medien
    Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 24 (1996), S. 523-524 
    Details
    ISSN: 0887-3585
    Schlagwort(e): esterase ; crystallography ; crystallization ; synchrotron radiation ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9 Å, b = 61.0 Å, c = 72.5 Å.
    Materialart: Digitale Medien
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  • 5
    Digitale Medien
    Digitale Medien
    Absolute configuration and conformation of the pure opioid antagonist (+)-2,9α-dimethyl-5-(m-hydroxyphenyl)morphan (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 4 (1992), S. 377-383 
    Details
    ISSN: 0899-0042
    Schlagwort(e): crystal structure ; molecular mechanics ; MM2-87 ; phenylmorphan ; phenyl-equatorial ; opioid ligand model ; μ-receptors ; K-receptors ; Chemistry ; Organic Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: (+)-2,9α-Dimethyl-5-(m-hydroxyphenyl)morphan is the only phenylmorphan analog whose affinity for opioid K-receptors is greater than its affinity for opioid κ-receptors. Pharmacologically, the compound is a pure opioid antagonist devoid of agonist activity in in vivo assays of antinociception. The absolute configuration of the compound has been determined to be (1R,5S,9R) from an X-ray crystallographic study of the chloride salt. Thus, the absolute configuration corresponds to that of the atypical opioid agonist (-)-phenylmorphan while the weak atypical agonist (-)-2,9α-dimethyl-5-(m-hydroxyphenyl)morphan corresponds to the potent morphine-like (+)-phenylmorphan. The preferred orientations of the phenyl ring for the two stereoisomers were determined using the molecular mechanics program MM2-87 and found to vary from that of the two parent compounds. The atypical properties of the two 9α-methyl analogs is consistent with an opioid ligand model which proposes that morphine-like properties require a particular range of phenyl orientations. There was good agreement between the structure obtained from X-ray crystallography and computed with the MM2-87 program. © 1992 Wiley-Liss, Inc.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/chir.530040608
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