Crystallization and preliminary X-ray diffraction analysis of the homodimeric form α2 of the HU protein from Escherichia coli
1999 ◽
Vol 55
(11)
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pp. 1952-1954
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The homodimeric form α2 of the Escherichia coli DNA-binding protein HU was crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystals belong to space group I222, with unit-cell parameters a = 31.09, b = 55.34, c = 117.63 Å, and contain one monomer per asymmetric unit. A full diffraction data set was collected to 2.3 Å resolution on a conventional X-ray source. The molecular-replacement method, using the HU crystallographic model from Bacillus stearothermophilus as a starting point, gave a reliable solution for the rotation and translation functions.
2014 ◽
Vol 70
(4)
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pp. 485-488
2014 ◽
Vol 70
(11)
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pp. 1566-1569
1999 ◽
Vol 55
(11)
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pp. 1920-1922
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2014 ◽
Vol 70
(5)
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pp. 608-610
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2014 ◽
Vol 70
(9)
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pp. 1244-1248
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2017 ◽
Vol 73
(11)
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pp. 601-606
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2013 ◽
Vol 69
(4)
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pp. 355-357
2015 ◽
Vol 71
(4)
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pp. 466-470
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2014 ◽
Vol 70
(4)
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pp. 535-537
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