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Despite possessing an N-terminal F-BAR domain, the srGAP2 protein regulates neurite outgrowth and neuronal migration by causing membrane protrusions reminiscent of the activity of I-BAR domain proteins. In this study, the F-BAR domain of human srGAP2 was crystallized and diffracted to 3.50 Å resolution.

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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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