Sensor-based Automated Continuous Grader for Spherical Fruits

244-253Weight grading is capable of more scrupulous separation than dimensional grading and reduces labor cost, damage, time, and power demand and also improves grading efficiency and accuracy. Hence a low-cost sensor-based grader for spherical fruits was developed and evaluated. The developed grader comprises of fruit feeding tray, fruit controlling shaft with gate arrangement, Electronic Control Unit (ECU), mainframe, belt conveyor, power transmission system, and collection baskets. The ECU consists of a load cell to sense the weight of the fruit, an amplifier to amplify the sensor data, a microcontroller to process the sensor signal and activate the corresponding motor and servo motors to push the fruit towards the basket by activating lever mounted on it. The machine is capable of weighing and grading the fruits into four different grades (grade I: >150 g, grade II: 130–150 g, grade III: 110–130 g and grade IV: <110 g), however, the grades can be altered as per the need by uploading in the program via USB cable. The grader was evaluated in terms of efficiency of grading, capacity and mechanical damage to the fruits at grader speeds of 3, 4, 5, and 6 rpm, respectively. The capacity of grader varied from 47.32 to 156.13 kg/h under different grader speeds. The developed grader is easy to operate and it doesn’t require skilled persons. It can be used for any spherical fruits and varying grades by changing the threshold values in the controller

Sensor-based Automated Continuous Grader for Spherical Fruits

Weight grading is capable of more scrupulous separation than dimensional grading and reduces labor cost, damage, time, and power demand and also improves grading efficiency and accuracy. Hence a low-cost sensor-based grader for spherical fruits was developed and evaluated. The developed grader comprises of fruit feeding tray, fruit controlling shaft with gate arrangement, Electronic Control Unit (ECU), mainframe, belt conveyor, power transmission system, and collection baskets. The ECU consists of a load cell to sense the weight of the fruit, an amplifier to amplify the sensor data, a microcontroller to process the sensor signal and activate the corresponding motor and servo motors to push the fruit towards the basket by activating lever mounted on it. The machine is capable of weighing and grading the fruits into four different grades (grade I: &gt;150 g, grade II: 130–150 g, grade III: 110–130 g and grade IV: &lt;110 g), however, the grades can be altered as per the need by uploading in the program via USB cable. The grader was evaluated in terms of efficiency of grading, capacity and mechanical damage to the fruits at grader speeds of 3, 4, 5, and 6 rpm, respectively. The capacity of grader varied from 47.32 to 156.13 kg/h under different grader speeds.  The developed grader is easy to operate and it doesn’t require skilled persons.  It can be used for any spherical fruits and varying grades by changing the threshold values in the controller

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Structure and genome release mechanism of human cardiovirus Saffold virus-3

In order to initiate an infection, viruses need to deliver their genomes into cells. This involves uncoating the genome and transporting it to the cytoplasm. The process of genome delivery is not well understood for non-enveloped viruses. We address this gap in our current knowledge by studying the uncoating of the non-enveloped human cardiovirus Saffold virus-3 (SAFV-3) of the family Picornaviridae SAFVs cause diseases ranging from gastrointestinal disorders to meningitis. We present a structure of a native SAFV-3 virion determined to 2.5 Å by X-ray crystallography and an 11 Å-resolution cryo-electron microscopy reconstruction of an "altered" particle that is primed for genome release. The altered particles are expanded relative to the native virus and contain pores in the capsid that might serve as channels for the release of VP4 subunits, N-termini of VP1, and the RNA genome. Unlike in the related enteroviruses, pores in SAFV-3 are located roughly between the icosahedral threefold and fivefold axes at an interface formed by two VP1 and one VP3 subunit. Furthermore, in native conditions many cardioviruses contain a disulfide bond formed by cysteins that are separated by just one residue. The disulfide bond is located in a surface loop of VP3. We determined the structure of the SAFV-3 virion in which the disulfide bonds are reduced. Disruption of the bond had minimal effect on the structure of the loop, but it increased the stability and decreased the infectivity of the virus. Therefore, compounds specifically disrupting or binding to the disulfide bond might limit SAFV infection. IMPORTANCE: A capsid assembled from viral proteins protects the virus genome during transmission from one cell to another. However, when a virus enters a cell the virus genome has to be released from the capsid in order to initiate infection. This process is not well understood for non-enveloped viruses. We address this gap in our current knowledge by studying the genome release of human Saffold virus-3. Saffold viruses cause diseases ranging from gastrointestinal disorders to meningitis. We show that before the genome is released, the Saffold virus-3 particle expands and holes form in the previously compact capsid. These holes serve as channels for the release of the genome and small capsid proteins VP4 that in related enteroviruses facilitate subsequent transport of the virus genome into the cell cytoplasm

Structure of the mycobacterial ESX-5 type VII secretion system pore complex

The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries