Engineering of recombinant crystallization chaperones
نویسندگان
چکیده
منابع مشابه
The use of recombinant methods and molecular engineering in protein crystallization.
Recombinant techniques are routinely used for the preparation of protein samples for structural studies including X-ray crystallography. Among other benefits, these methods allow for a vast increase in the amount of obtained protein as compared to purification from source tissues, ease of purification when fusion proteins containing affinity tags are used, introduction of SeMet for phasing, and...
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A glycosylation-minus mutant of rat cathepsin B expressed in yeast has been purified and crystallized. X-ray diffraction data have been collected and molecular replacement for solving the structure is in progress. The space group for the recombinant rat cathepsin B was determined to be P2(1) with unit cell dimensions alpha = 62.2 A, b = 90.19 A, c = 47.07 A, and beta = 97.43 degrees. A unit cel...
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Although many methods have been proposed for engineering services and customer solutions, most of these approaches give little consideration to recombinant service innovation. In an age of smart products and smart data, we can, however, expect that many of future service innovations need to be based on adding, transferring, dissociating, and associating existing value propositions. The purpose ...
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Protein crystallization remains a key limiting step in the characterization of the atomic structures of proteins and their complexes by X-ray diffraction methods. Current data indicate that standard screening procedures applied to soluble well folded prokaryotic proteins yield X-ray diffraction crystals with an approximately 20% success rate and for eukaryotic proteins this figure may be signif...
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An Escherichia coli expression system has been developed for pea cytosolic ascorbate peroxidase (APX). The enzyme was expressed as a fusion product with the E. coli maltose-binding protein for rapid, affinity chromatography purification. Recombinant ascorbate peroxidase (rAPX) was purified by tryptic digestion to separate the maltose-binding protein from rAPX followed by three chromatographic s...
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ژورنال
عنوان ژورنال: Current Opinion in Structural Biology
سال: 2009
ISSN: 0959-440X
DOI: 10.1016/j.sbi.2009.04.008