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Crystals of Deg8, an ATP-independent serine endopeptidase from A. thaliana, were monoclinic, belonging to space group C2 with unit-cell parameters a = 129.5, b = 124.2, c = 93.3 Å, β = 132.4°, and diffracted to 2.0 Å resolution.

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Crystals of EtFPOX from E. terrenum sp. diffracted to 1.9 Å resolution and belonged to space group P212121, with unit-cell parameters a = 65.6, b = 80.0, c = 83.4 Å.

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The complex of Arf1-GDP and dimeric p23 peptide, which is likely to be involved in membrane binding of Arf1, has been crystallized and preliminary crystallographic analysis was performed.
Keywords: Arf1; p23; COPI; dimer.

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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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