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17 citations found for Shin, C.

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Unmodified, active human TRAIL (Apo-2L) has been crystallized. Initial results indicate that the cytokine is a homotrimer.

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Contrary to the general concept, the archaeal Smc-based complex appears to lack the kite subunit ScpB that is essential in the bacterial Smc–ScpAB complex that mediates chromosome organization.

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Acta Cryst. (2023). A79, C831
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The psychrophilic esterase PsEst3 was successfully overexpressed using a psychrophilic chaperonin co-expression system, and was cystallized using the vapour-diffusion method. The X-ray diffraction data were collected to 2.1 Å resolution.

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The structure of the title compound was determined by single-crystal X-ray methods. The carbonyl C=O bond distances are approximately 1.20 Å and van der Waals intermolecular contacts are normal. The bond distances are normal for all bonds in the molecule except for those involving C9: the C-F bond distance is 1.382 (6) Å, and the C-C bond distances are 1.545 (8), 1.531 (8) and 1.529 (9) Å, all approximately 0.05 Å longer than normal for these bonds.

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The crystal structure of the FERM domain of protein tyrosine phosphatase non-receptor type 21, a regulator of cancer progression and invasion, was determined and an atomic-level structural analysis was conducted.

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A bunch-by-bunch measurement system has been developed at Pohang Light Source II, consisting of a four-channel button pick-up, 20 GHz sampling oscilloscope and an 800 MHz low-pass digital filter.

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The title compound, [Fe(C44H8F20N4)]·2C6H6, contains a four-coordinated FeII atom, which lies on a center of symmetry. The porphyrin macrocycle is planar, and the Fe-N bond distances are in the range 1.9891 (13)-1.9982 (13) Å. The spin state of the FeII atom is intermediate (S = 1), as confirmed by NMR spectroscopy. The asymmetric unit contains two half benzene mol­ecules, each lying about an independent inversion centre; one of the benzene rings is located just below (and by inversion symmetry, another is just above) the Fe atom, where it interacts weakly with the porphyrin ring.


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The coiled-coil domain of human PIST was crystallized at 293 K and diffracted to a resolution of 4.0 Å. The crystals were found to belong to space group P6222 or P6422, with unit-cell parameters a = b = 85.19, c = 240.09 Å, γ = 120.00°.

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Rab6A'(Q72L), a constitutively active GTP-binding form of Rab6A, was purified and crystallized. The crystals were found to belong to space group P22121, with unit-cell parameters a = 36.84, b = 96.78, c = 109.99 Å. The crystals were obtained at 293 K and diffracted to a resolution of 1.9 Å.

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Crystal structures of PsEst3 complexed with various ligands and its biochemical characterization indicate the emergence of a new GHSR-type lipase/esterase and reveal the relationship between its structure and function.

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The crystal structure of the Cmr1 subunit of the Cmr interference complex reveals a single-stranded RNA-binding site and an associated ribonuclease activity.


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