Abstract: The invention includes a mutant T7 DNA ligase or a biologically active fragment thereof, which has greater activity than wild type T7 DNA ligase. The mutant T7 DNA ligase, or the biologically active fragment, has one or more substitutions differing from the wild type, as described more fully in the Summary. The preferred mutant T7 DNA ligase has at least one of the following mutations: E63K (SEQ ID NO:4), K73E (SEQ ID NO:6), K137E (SEQ ID NO:7), K174E (SEQ ID NO:9), E182K (SEQ ID NO:11), K210E (SEQ ID NO: 13), E243K (SEQ ID NO:15), D245R (SEQ ID NO: 17), E268K (SEQ ID NO:19), E272K (SEQ ID NO:21), E289K (SEQ ID NO:23), K295E (SEQ ID NO:25) and D336R (SEQ ID NO:27).

Abstract: A number of T4 DNA ligase mutants exhibiting enhanced ligation activity in the presence of high salt concentrations compared to the wild-type ligase were engineered, characterized, and selected via gel electrophoresis of ligation products from a standard ligation assay. Ligase catalyzes the formation of phosphodiester bonds between the 5? and 3? ends of complementary cohesive ends or blunt ends of duplex DNA, a process that is vital to numerous molecular biology processes including cloning and sequencing.

Abstract: The invention relates to covalently bonding a protein/polypeptide with lower thermostability to a target protein with higher thermostability can reduce thermostability (increase thermolability) of the target protein. Thereafter, the target protein function can be deactivated by either heating it, even to a relatively low temperature, or by carrying out a reaction with it in the reaction mixture, at high temperature. Either way, the target protein's function is inactivated, thus reducing some of its long-acting side activity. This method for reducing thermostability of a target protein can inhibit the star activity of any restriction enzyme, including but not limited to BsaI.

Abstract: The invention includes a mutant Taq polymerase, which can significantly extend and amplify a target sequence where the extension conditions are time limited to as little as one second. The mutant Taq polymerase, or a biologically active fragment thereof, has one or more substitutions differing from the wild type as shown in Table I.

Abstract: An improved method of site directed mutagenesis on plasmids by PCR is described, where at least two mutations are added to the parts of the plasmid DNA by site direct mutagenesis. One mutation is an intended mutation, and the other mutation changes the function of the mutated plasmid from the function of the template plasmid. The functional change is one to allow reduction of the retention of non-integrated template DNA, even in the absence of wild type template digestion with DpnI.

Abstract: The invention includes a mutant Taq polymerase, which can effectively amplify a target sequence under conditions of salt concentration(s) similar to body fluids, including blood, serum or plasma preserved with sodium citrate. The mutant Taq polymerase, or a biologically active fragment thereof, has one or more substitutions differing from the wild type as shown in Table I.

Abstract: Automatic terrain evaluation of landing surfaces, and associated systems and methods are disclosed herein. A representative method includes receiving a request to land a movable object and, in response to the request, identifying a target landing area on a landing surface based on at least one image of the landing surface obtained by the movable object. The method can further include directing the movable object to land at the target landing area.

Abstract: Disclosed is a novel T7 DNA ligase mutant with the mutation R129D, that had higher specificity toward cohesive end-ligation even in the presence of polyethylene glycol. Controlling the composition of final ligation products is important and thus, a variant which improves the specificity of T7 DNA ligase to cohesive ends will generate more reliable results.

Abstract: Disclosed is using a TEV protease (wild type or mutant) suited for removal from a reaction mixture, wherein the TEV protease displays a dual affinity tag including a chitin binding domain (CBD) tag and a histidine tag, preferably where the CBD tag precedes the N-terminus of the protease and the CBD tag is preceded by the histidine tag, which is preferably a 6-mer histidine tag; and optionally further including linkers, preferably Gly-Ser linkers, and more preferably a 6-mer Gly-Ser linker, between the tags. A linker, also preferably a Gly-Ser linker, can also follow the CBD tag and precede the protease portion. In certain embodiments, no such linkers are present and in other embodiments, only one such linker is present.

Abstract: Taq DNA polymerase mutants exhibiting reverse transcriptase activity compared to wild type polymerase were engineered, characterized, and selected via polymerase chain reactions visualized via electrophoresis on agarose gels. Initial screening was followed up with probe-based qualitative, real-time PCR (qPCR) with a typical reverse transcription cycling protocol to detect specified ribonucleic acid (RNA) target sequences. The engineered variants can render robust cDNA from RNA target substrates and amplify that cDNA under standard reaction conditions without the assistance of added reverse transcriptase enzymes.

Abstract: Disclosed are Taq DNA polymerase mutants which exhibit enhanced efficiency in qPCR compared to the wild type Taq DNA polymerase. Such mutants include: V62S, V64S, A70F, F73A, A77F, P253G, E255K, D257R, A259F, A271F, L288S, E289K, S357I, L361S, L376S, P382G, T385I, G418P, R419D, E421K, L461S, A472F, E497K, L498S, E524K, D551R, R556D, S679I, L789S, E189K/E507K/E742K (See Sequence Listing Guide for the mutants' amino acid and protein sequences).

Abstract: Computing platforms and related methods for providing accessible user interfaces are disclosed. An example apparatus includes a display controller to a display controller to sample a region of a display frame associated with a location of a touch on a display screen of a user device and logic circuitry to, after a Basic Input Output System (BIOS) is operational in the user device and prior to loading of an operating system of the user device, identify content in the display region and cause at least one output device to generate an output representative of the content, the output including at least one of an audible output or a haptic output.

Abstract: Methods and compositions are provided for engineering mutant enzymes with reduced star activity where the mutant enzymes have a fidelity index (FI) in a specified buffer that is greater than the FI of the non-mutated enzyme in the same buffer.

Abstract: Compositions and methods are provided for enzymes with altered properties that involve a systematic approach to mutagenesis and a screening assay that permits selection of the desired proteins. Embodiments of the method are particularly suited for modifying specific properties of restriction endonucleases such as star activity. The compositions includes restriction endonucleases with reduced star activity as defined by an overall fidelity index improvement factor.

Abstract: Disclosed are Taq DNA polymerase mutants which exhibit enhanced efficiency in qPCR compared to the wild type Taq DNA polymerase. Such mutants include: V62S, V64S, A70F, F73A, A77F, P253G, E255K, D257R, A259F, A271F, L288S, E289K, S357I, L361S, L376S, P382G, T385I, G418P, R419D, E421K, L461S, A472F, E497K, L498S, E524K, D551R, R556D, S679l, L789S, E189K/E507K/E742K (See Sequence Listing Guide for the mutants' amino acid and protein sequences).

Abstract: Either wild type or mutant Serratia marcescens Nuclease (“SMN”) is engineered to display a C-terminal Chitin Binding Domain (CBD-tag), followed, at the C-terminus side of the CBD-tag, by a poly-histidine tag (His-tag), where the His-tag is preferably a 6-mer and preferably is preceded by a Gly-Ser linker, thereby generating a recombinant SMN protein that retains dual affinity tags (a CBD-tag and a His-tag) at the C-terminus, to make it easily removed from a reaction solution following digestion of nucleic acids in the reaction mixture. It can also be used for binding SMN to a solid support for use in nucleic acid digestion in a sample contacted with the solid support.

Abstract: Methods and compositions are provided for engineering mutant enzymes with reduced star activity where the mutant enzymes have a fidelity index (FI) In a specified buffer that is greater than the FI of the non-mutated enzyme in the same buffer.

Abstract: Compositions and methods are provided for enzymes with altered properties that involve a systematic approach to mutagenesis and a screening assay that permits selection of the desired proteins. Embodiments of the method are particularly suited for modifying specific properties of restriction endonucleases such as star activity. The compositions includes restriction endonucleases with reduced star activity as defined by an overall fidelity index improvement factor.

Abstract: The invention includes a mutant T7 DNA ligase or a biologically active fragment thereof, which has greater activity than wild type T7 DNA ligase, on a blunt-ended dsDNA substrate. The mutant T7 DNA ligase, or the biologically active fragment, has one or more substitutions differing from the wild type, which are E63K (SEQ ID NO:3; SEQ ID NO:4), D132R (SEQ ID NO:5; SEQ ID NO:6), E243K (SEQ ID NO:7; SEQ ID NO: 8), D245R (SEQ ID NO:9; SEQ ID NO: 10), E272K (SEQ ID NO:11; SEQ ID NO: 12), D288R (SEQ ID NO:13; SEQ ID NO:14), E289K (SEQ ID NO:15; SEQ ID NO: 16), and E292K (SEQ ID NO:17; SEQ ID NO:18).

Abstract: The invention relates to a seamless cloning method, comprising a single assembly step of two or more polynucleotides, e.g., a plasmid vector and a gene insert, conducted at 58 to 100° C., the preferred temperature(s) being the same or greater than a particular one of the following temperatures: 58° C., 59° C., 60° C., 61° C., 62° C., 63° C., 64° C., 65° C., 66° C., 67° C., 68° C., 69° C., 70° C., 71° C., 72° C., 73° C., 74° C., 75° C., 76° C., 77° C., 78° C., 79° C., 80° C., 84° C., 88° C., 92° C., 96° C. and 100° C., and a transformation into chemically competent cells for covalent linking, preferably including a static recovery period.