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The head domain of the DNA-repair protein RecN from D. radiodurans, composed of the amino- and carboxy-terminal domains, was crystallized. X-ray diffraction data were collected to 3.0 Å resolution and the crystals belonged to space group P21.

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The coiled-coil domain of the essential DNA-repair protein RecN from D. radiodurans was crystallized. The crystals belonged to space group P21 and diffracted X-rays to 2.04 Å resolution.

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A hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase involved in chlorogenic acid biosynthesis in C. canephora was crystallized using the vapour-diffusion method. A diffraction data set was collected to 3.0 Å resolution on the microfocus beamline (ID23-2) at ESRF and a structure solution was obtained using molecular replacement.
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