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The Escherichia coli cyclic AMP receptor protein (CRP) crystals were obtained and diffracted at a 2.9 Å resolution, which belonged to the space group P3121, with unit-cell parameters a = b = 76.03, c = 144.00 Å. The asymmetric unit was found to contain one protein molecule and a half 38 bp full-length double-stranded DNA fragment with a Matthews coefficient of 2.62 Å3 Da-1 and a solvent content of 53.14%.

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The Escherichia coli cyclic AMP receptor protein (CRP) is a prokaryotic global transcription activator protein that controls the expression of many different genes. cAMP-free D53H CRP crystals were obtained and diffracted at a resolution of 2.9 Å. Based on the systematic absences of the crystals, the likely space group is P212121 with the unit-cell parameters a = 76.66, b = 152.14, and c = 176.11 Å. The asymmetric unit was confirmed to contain four protein dimers with a Matthews coefficient of 2.71 Å3 Da-1 and a solvent content of 54.68%.
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