18 research outputs found

    Growth of bulk single-crystal MnP helimagnet and its structural and NMR characterization

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    Bulk single crystals of manganese phosphide (MnP) were grown from melt at 1 GPa and 1200 C by using a cubic-anvil, high-pressure, and high-temperature technique. The obtained black colored crystals exhibit a plate-like morphology, with flat surfaces and maximum dimensions up to 4 x 2 x 0.5 mm3. The orthorhombic crystal structure was confirmed by X-ray diffraction [Pnma, 62, Z = 4, a = 5.2510(4) {\AA}, b = 3.1670(3) {\AA}, c = 5.90098 (4) {\AA} and V = 98.279(14) {\AA}3]. Temperature-dependent magnetization measurements reveal the occurrence of two successive transitions: a paramagnetic to ferromagnetic transition at Tc = 290.5 K and the development of a double helimagnetic order at Ts = 44.5 K. Zero-field 31P NMR measurements in the FM and in the screw-spin AFM state show prominent features, which are compared with previous experimental data and theoretical calculations. The relatively large crystals obtained here open up new possibilities for further explorations of this interesting material.Comment: 4 tables, 7 figure

    Rapid Generation of Monoclonal Antibodies from Single B Cells by Ecobody Technology

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    Single B cell sampling following to direct gene amplification and transient expression in animal cells has been recognized as powerful monoclonal antibodies (mAbs) screening strategies. Here we report Ecobody technology which allows mAbs screening from single B cells in two days This technology uses Escherichia coli cell-free protein synthesis (CFPS) for mAb expression. In the CFPS step, we employed our original techniques: (1) ‘Zipbody’ as a modified Fab (fragment of antigen binding) format, in which the active Fab formation is facilitated by adhesive leucine zipper peptides fused at the C-termini of the light and heavy chains; and (2) an N-terminal SKIK peptide tag that can markedly increase protein production. By the Ecobody technology, we demonstrated rapid screening of antigen specific mAbs from immunized rabbits and Epstein-Barr Virus infected human B cells. We further obtained rabbit mAbs in E. coli expression system yielding to 8.5 mg of purified proteins from 1 L bacterial culture
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