Crystallization and preliminary X-ray characterization of aminopeptidase N fromEscherichia coli
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چکیده
منابع مشابه
Crystallization and preliminary X-ray diffraction
The amyloidogenic Leu55Pro variant of transthyretin has been expressed, purified and crystallized in space group C2. The cell constants are a--149.99, b = 78.74, c = 98.95A, = 100.5 ° and the crystals diffract to 2.7,~ resolution. There are eight monomers in the asymmetric unit giving a V M = 2.6,~,3 Da -w and 53% solvent content. In the wild-type protein, the crystals are orthorhombic with two...
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4.5S RNA forms with Ffh protein the prokaryotic signal recognition particle (SRP), a highly conserved ribonucleoprotein complex essential for protein secretion. It also independently binds to elongation factor G (EF-G) in the ribosome and has a function in a subset of translocation events that is transient but required for viability. Crystals of three different constructs encompassing the conse...
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Pili are key cell-surface components that allow the attachment of bacteria to both biological and abiotic solid surfaces, whilst also mediating interactions between themselves. In Escherichia coli, the common pilus (Ecp) belongs to an alternative chaperone-usher (CU) pathway that plays a major role in both early biofilm formation and host-cell adhesion. The chaperone EcpB is involved in the bio...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2006
ISSN: 1744-3091
DOI: 10.1107/s1744309106021567