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23 citations found for MORENO, A.

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Different crystallization techniques such as vapour diffusion in hanging drops and counterdiffusion in gels allowed the selective isolation of different crystal polymorphs of the SdsA protein from Pseudomonas aeruginosa PAO1 and improved their diffraction quality. Analysis of the three-dimensional structures obtained from the different polymorphs provided insights into the relevance of crystal packing for the interpretation of biological information.

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Rietveld refinement of X-ray diffraction data and dilatometry performed as a function of annealing time for L-asparagine monohydrate confirmed that the phase transition associated with loss of the water molecule (anhydrous phase) is time dependent.

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This article describes protein crystallization under the influence of an electric field using a sitting-drop and vapor-diffusion experimental setup.

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The observation of a repetitive pattern obtained for protein crystals formed by reaction-diffusion in capillary tubes is reported for the first time.

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Lysozyme single crystals were grown with their shape controlled by the cylindrical capillary used as a growth cell. The shaped crystals were shown to diffract up to 1.74 Å.

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It is shown that the precipitating agents commonly used in protein crystal growth can be used in the gel acupuncture method. Silica and agar gels are recommended for this method. The results are illustrated for the growth of lysozyme, concanavalin A and ribonuclease.

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The influence of an internal electric field upon the protein structure of crystals grown inside capillary tubes is evaluated during the crystallization process by means of the gel-acupuncture method using lysozyme and thaumatin.


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Minute amounts of protein impurities alter the growth of aspartyl-tRNA synthetase crystals. With the purest enzyme, the best crystals are grown in environments where convection is reduced.

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This note focuses on two different ways of enhancing the use of gels in protein crystallization by applying oils to the trials.

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The influence of an external applied potential on the growth of ferritin crystals from horse spleen is described.

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C-Phycocyanin (C-PC) and allophycocyanin (APC) from Spirulina platensis have been purified and crystallized by the gel-acupuncture technique. The crystals of APC belong to space group P6322 and C-PC crystals belong to either space group P6 or P63.


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Using the implementation of the gel-acupuncture technique, crystal growth rates, as a function of the supersaturation along capillary tubes, were measured.

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Acta Cryst. (1996). A52, C512
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The structure of the tyrosine aminotransferase from the parasitic protozoa L. infantum was solved to 2.35 Å resolution. The difference in substrate specificity and enzymatic activity between leishmanial and mammalian TAT is explained based on the presence of two residues (Gln55 and Asn58).

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The title compound, [Ir4(C5H5N)(CO)11], shows a tetra­hedral Ir4 core in which each Ir atom is linked to three other Ir atoms and three terminal carbonyl groups, except for one Ir atom, which carries two carbonyl ligands and one N-coordinated pyridine mol­ecule. An intricate set of C—H...π hydrogen bonds stabilizes the crystal packing, where the π-systems are those of the C[triple bond]O bonds of the carbonyl ligands.

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This report describes the application of organic solvent gels and aqueous hydrogels for crystallization of soluble and membrane proteins. The hydrogel is based on polyvinyl alcohol and the organic based gels are formed using polyethylene oxide, which is compatible with a variety of solvents. Diffracting crystals were obtained with both gel systems.

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The purification, crystallization and preliminary X-ray diffraction data of the protein struthiocalcin 1 isolated from ostrich eggshell are reported.

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The crystal structure of struthiocalcin-1 (SCA-1) from ostrich eggshell has been determined in two different crystal forms at 1.50 Å resolution, displaying the characteristic C-type lectin-like fold with a surface decorated with acidic residues, highlighting the overall negative charge of SCA-1.

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