Switching performance of epitaxially grown normally-off 4H-SiC JFET

Static and dynamic behavior of the epitaxially grown dual gate trench 4H-SiC junction field effect transistor (JFET) is investigated. Typical on-state resistance Ron was 6-10mΩcm2 at VGS = 2.5V and the breakdown voltage between the range of 1.5-1.8kV was realized at VGS = -5V for normally-off like JFETs. It was found that the turn-on energy delivers the biggest part of the switching losses. The dependence of switching losses from gate resistor is nearly linear, suggesting that changing the gate resistor, a way similar to Si-IGBT technology, can easily control di/dt and dv/dt. Turn-on losses at 200°C are lower compared to those at 25°C, which indicates the influence of the high internal p-type gate layer resistance. Inductive switching numerical analysis suggested the strong influence of channel doping conditions on the turn-on switching performance. The fast switching normally-off JFET devices require heavily doped narrow JFET channel design. © (2009) Trans Tech Publications, Switzerland.

Copurification of the Lac repressor with polyhistidine-tagged proteins in immobilized metal affinity chromatography.

One of the commonly used resins for immobilized metal affinity purification of polyhistidine-tagged recombinant proteins is TALON resin, a cobalt (II)--carboxymethylaspartate-based matrix linked to Sepharose CL-6B. Here, we show that TALON resin efficiently purifies the native form of Lac repressor, which represents the major contaminant when (His)(6)-tagged proteins are isolated from Escherichia coli host cells carrying the lacI(q) gene. Inspection of the crystal structure of the repressor suggests that three His residues (residues 163, 173, and 202) in each subunit of the tetramer are optimally spaced on an exposed face of the protein to allow interaction with Co(II). In addition to establishing a more efficient procedure for purification of the Lac repressor, these studies indicate that non-lacI(q)-based expression systems yield significantly purer preparations of recombinant polyhistidine-tagged proteins.