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Expression, purification, crystallization and preliminary X-ray analysis of YaeQ (XAC2396) from Xanthomonas axonopodis pv. citri
Xanthomonas axonopodis pv. citri YaeQ (XAC2396) is a member of a family of bacterial proteins conserved in several Gram‐negative pathogens. Here, the cloning, expression, purification and crystallization of the 182‐residue (20.6 kDa) YaeQ protein are described. Recombinant YaeQ containing selenometh...
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Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-05, Vol.61 (5), p.493-495 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | Xanthomonas axonopodis pv. citri YaeQ (XAC2396) is a member of a family of bacterial proteins conserved in several Gram‐negative pathogens. Here, the cloning, expression, purification and crystallization of the 182‐residue (20.6 kDa) YaeQ protein are described. Recombinant YaeQ containing selenomethionine was crystallized in space group P21 and crystals diffracted to 1.9 Å resolution at a synchrotron source. The unit‐cell parameters are a = 39.75, b = 91.88, c = 48.03 Å, β = 108.37°. The calculated Matthews coefficient suggests the presence of two YaeQ molecules in the asymmetric unit. Initial experimental phases were calculated by the multiple‐wavelength anomalous dispersion technique and an interpretable electron‐density map was obtained. |
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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309105010985 |