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The expression, purification, crystallization and preliminary crystallographic analysis of the high-mobility group protein (HMO2) from S. cerevisiae are reported.

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Immunity protein TsiV3 from Vibrio cholera has been expressed, purified and crystallized. The crystal belonged to space group P212121, with unit-cell parameters a = 73.3, b = 78.12, c = 106.18 Å and diffract to 2.55 Å resolution.

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A reductive methylation-modified RRF from Thermoanaerobacter tengcongensis (TteRRF) has been crystallized using the vapour-diffusion method. The crystal belonged to space group P6122/P6522 with unit-cell parameters a = b = 103.26, c = 89.17 Å.

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Here, the expression, purification, crystallization and preliminary crystallographic analysis of putative protein PA5088 from Pseudomonas aeruginosa are reported.

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McbB, a multifunctional enzyme responsible for catalysing Pictet–Spengler cyclization, decarboxylation and oxidation reactions in the biosynthesis of β-carboline, was expressed and crystallized. The crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 66.06, b = 85.48, c = 106.19 Å, α = 90.00, β = 106.77, γ = 90.00°.

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McbB, a multifunctional enzyme responsible for catalysing Pictet–Spengler cyclization, decarboxylation and oxidation reactions in the biosynthesis of β-carboline, was expressed and crystallized. The crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 66.06, b = 85.48, c = 106.19 Å, α = 90.00, β = 106.77, γ = 90.00°.
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