mosquito crystallization robot  (SPT Labtech)


Bioz Verified Symbol SPT Labtech is a verified supplier
Bioz Manufacturer Symbol SPT Labtech manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 96

    Structured Review

    SPT Labtech mosquito crystallization robot
    Mosquito Crystallization Robot, supplied by SPT Labtech, used in various techniques. Bioz Stars score: 96/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mosquito crystallization robot/product/SPT Labtech
    Average 96 stars, based on 40 article reviews
    Price from $9.99 to $1999.99
    mosquito crystallization robot - by Bioz Stars, 2022-09
    96/100 stars

    Images

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 96
    SPT Labtech mosquito lcp
    KEK-style membrane sandwich <t>LCP</t> crystallization. ( a ) A KEK original adaptor (bottom) is in the <t>SBS</t> format and can be used with PXS2 because the adaptor is compatible with the KEK crystallization plate. A film sandwich LCP plate supported by glass plates (top) fits onto the adaptor. ( b ) Schematic drawing of a cross section of the KEK-style LCP plate. ( c ) Comparison of the crystallization-drop images under a polarized condition between glass-supported (KEK-style, left) and plastic-supported (MD Diffrax, right) LCP plates.
    Mosquito Lcp, supplied by SPT Labtech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mosquito lcp/product/SPT Labtech
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mosquito lcp - by Bioz Stars, 2022-09
    96/100 stars
      Buy from Supplier

    Image Search Results


    KEK-style membrane sandwich LCP crystallization. ( a ) A KEK original adaptor (bottom) is in the SBS format and can be used with PXS2 because the adaptor is compatible with the KEK crystallization plate. A film sandwich LCP plate supported by glass plates (top) fits onto the adaptor. ( b ) Schematic drawing of a cross section of the KEK-style LCP plate. ( c ) Comparison of the crystallization-drop images under a polarized condition between glass-supported (KEK-style, left) and plastic-supported (MD Diffrax, right) LCP plates.

    Journal: Acta Crystallographica. Section F, Structural Biology Communications

    Article Title: A fully automated crystallization apparatus for small protein quantities

    doi: 10.1107/S2053230X20015514

    Figure Lengend Snippet: KEK-style membrane sandwich LCP crystallization. ( a ) A KEK original adaptor (bottom) is in the SBS format and can be used with PXS2 because the adaptor is compatible with the KEK crystallization plate. A film sandwich LCP plate supported by glass plates (top) fits onto the adaptor. ( b ) Schematic drawing of a cross section of the KEK-style LCP plate. ( c ) Comparison of the crystallization-drop images under a polarized condition between glass-supported (KEK-style, left) and plastic-supported (MD Diffrax, right) LCP plates.

    Article Snippet: The protein sample is provided in an SBS-formatted 384-well plate which is supplied to the mosquito LCP.

    Techniques: Crystallization Assay

    Involvement of TM4 in the substrate cleavage and dependence on residue D446 (a) Amino acid sequence alignment of the C-terminal regions of nine RseP orthologues classified as γ -proteobacteria. The UniProtKB accession number of each orthologue is shown (Ec, Escherichia coli ; Kk, Kangiella koreensis ; Se, Salmonella enterica serovar Typhimurium; Yp, Yersinia pestis ; Vc, Vibrio cholerae ; Hi, Haemophilus influenzae ; Pm, Pasteurella multocida ; Pa, Pseudomonas aeruginosa ; Xf, Xylella fastidiosa ). Conserved and similar residues are boxed in black and gray, respectively. The positions of TM segments, structural elements and two featured residues are shown based on those of Ec RseP. (b) Complementation assay. Cultures of E. coli KK31 [Δ rseP /pKK6 (PBAD- rseP )] cells carrying plasmids for Ec RseP (pYH825) or its variants were serially diluted and spotted on L agar plates containing IPTG (left) to test complementation or containing L-arabinose (right) as a control for total-cell count. A representative result from three biological replicates is shown. ΔTM4 and ΔCTail indicate the F426amber and D446amber mutations, respectively. (c) In vivo cleavage assay with long induction. E. coli KA306 (Δ rseA Δ rseP Δ clpP ) cells harboring one plasmid for HA-MBP-RseA148 (pKA65) and one for Ec RseP (pYH825) or its variants were grown at 30°C for 3 h with 1 mM IPTG and 1 mM cAMP in M9-based medium. The cleavage efficiency was determined from immunoblots (images) as in Fig 2e . Bar plots and error bars represent the means ± S.D. from three biological replicates. (d) Conserved residues on TM4. The residues shown as sphere models were mutated to alanine (A442 was mutated to serine) to examine their roles in the proteolytic activity, as shown in Fig. S14. Another mutated residue, R449, was disordered in the electron density map as indicated by dotted lines. The ΔTM4 mutant in (b) lacks the C-terminal residues downstream of F426 (white sphere) while ΔCTail lacks the periplasmic tail region (D446 to the C-terminus). Batimastat and active site residues are shown as stick models. The zinc ion is shown as a sphere. (e) Specific interaction between D446 and PCT-H2. TM4 and the PCT-loop, including PCT-SH and PCT-H2, are shown as stick models in magenta, pink, and salmon, respectively. D446 interacts with the electropositive N-terminal end of the PCT-H2 helix dipole where the side chain of D446 and the main chain N-H group of S363 (each in white) form a hydrogen bond.

    Journal: bioRxiv

    Article Title: Mechanistic insights into intramembrane proteolysis by E. coli site-2 protease homolog RseP

    doi: 10.1101/2022.01.31.478169

    Figure Lengend Snippet: Involvement of TM4 in the substrate cleavage and dependence on residue D446 (a) Amino acid sequence alignment of the C-terminal regions of nine RseP orthologues classified as γ -proteobacteria. The UniProtKB accession number of each orthologue is shown (Ec, Escherichia coli ; Kk, Kangiella koreensis ; Se, Salmonella enterica serovar Typhimurium; Yp, Yersinia pestis ; Vc, Vibrio cholerae ; Hi, Haemophilus influenzae ; Pm, Pasteurella multocida ; Pa, Pseudomonas aeruginosa ; Xf, Xylella fastidiosa ). Conserved and similar residues are boxed in black and gray, respectively. The positions of TM segments, structural elements and two featured residues are shown based on those of Ec RseP. (b) Complementation assay. Cultures of E. coli KK31 [Δ rseP /pKK6 (PBAD- rseP )] cells carrying plasmids for Ec RseP (pYH825) or its variants were serially diluted and spotted on L agar plates containing IPTG (left) to test complementation or containing L-arabinose (right) as a control for total-cell count. A representative result from three biological replicates is shown. ΔTM4 and ΔCTail indicate the F426amber and D446amber mutations, respectively. (c) In vivo cleavage assay with long induction. E. coli KA306 (Δ rseA Δ rseP Δ clpP ) cells harboring one plasmid for HA-MBP-RseA148 (pKA65) and one for Ec RseP (pYH825) or its variants were grown at 30°C for 3 h with 1 mM IPTG and 1 mM cAMP in M9-based medium. The cleavage efficiency was determined from immunoblots (images) as in Fig 2e . Bar plots and error bars represent the means ± S.D. from three biological replicates. (d) Conserved residues on TM4. The residues shown as sphere models were mutated to alanine (A442 was mutated to serine) to examine their roles in the proteolytic activity, as shown in Fig. S14. Another mutated residue, R449, was disordered in the electron density map as indicated by dotted lines. The ΔTM4 mutant in (b) lacks the C-terminal residues downstream of F426 (white sphere) while ΔCTail lacks the periplasmic tail region (D446 to the C-terminus). Batimastat and active site residues are shown as stick models. The zinc ion is shown as a sphere. (e) Specific interaction between D446 and PCT-H2. TM4 and the PCT-loop, including PCT-SH and PCT-H2, are shown as stick models in magenta, pink, and salmon, respectively. D446 interacts with the electropositive N-terminal end of the PCT-H2 helix dipole where the side chain of D446 and the main chain N-H group of S363 (each in white) form a hydrogen bond.

    Article Snippet: 50 or 100 nL aliquots of the protein-monoolein mixture were dispensed onto 96-well glass plates and overlaid with 800 nL of crystallization solution using a mosquito LCP (TTP LabTech) or Crystal Gryphon LCP (Art Robbins Instruments).

    Techniques: Sequencing, Cell Counting, In Vivo, Cleavage Assay, Plasmid Preparation, Western Blot, Activity Assay, Mutagenesis

    mRNA sequence of rat aromatase. Exon boundaries in the rat mRNA sequence of cytochrome P450 (NCBI Reference Sequence: NM_017085.2) are marked in bold and highlighted in grey. An arrow indicates beginning of the translated region in the long form of aromatase. Untranslated regions have been grayed out. The 90 bp fragment (715–805) that was amplified in our qPCR and RT-PCR analyses is highlighted in yellow. The region that is thought to be missing in the truncated form of the enzyme involves the exons 2 and 3 and hence encompasses the sequence that was targeted in our study. The boxed nucleotides in the sequence indicate the start and the end of the RNA probe that protected only the long form of aromatase in ribonuclease protection assays [10] .

    Journal: PLoS ONE

    Article Title: Quantitative Analysis of Long-Form Aromatase mRNA in the Male and Female Rat Brain

    doi: 10.1371/journal.pone.0100628

    Figure Lengend Snippet: mRNA sequence of rat aromatase. Exon boundaries in the rat mRNA sequence of cytochrome P450 (NCBI Reference Sequence: NM_017085.2) are marked in bold and highlighted in grey. An arrow indicates beginning of the translated region in the long form of aromatase. Untranslated regions have been grayed out. The 90 bp fragment (715–805) that was amplified in our qPCR and RT-PCR analyses is highlighted in yellow. The region that is thought to be missing in the truncated form of the enzyme involves the exons 2 and 3 and hence encompasses the sequence that was targeted in our study. The boxed nucleotides in the sequence indicate the start and the end of the RNA probe that protected only the long form of aromatase in ribonuclease protection assays [10] .

    Article Snippet: The PCR reactions were prepared in triplicate in a 384-well plate by mixing 1.2 µl cDNA (10 µg) and 1.2 µl commercially available GoTaq qPCR master mix (Promega) using a Mosquito LCP automated liquid handler (TTP Labtech) and then adding 10 nl primer mix (for 200 nM of each primer in the final reaction) with an Echo Liquid Handler (Labcyte). qPCR was carried out using the following program: 95°C for 5 min, 40 cycles of 95°C for 15 sec and 60°C for 1 min, and a melt curve analysis (95°C for 15 sec, 60°C to 95°C with 0.5°C intervals, 30 sec per interval).

    Techniques: Sequencing, Amplification, Real-time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction

    Effect of gonadal/hormonal status on aromatase mRNA expression in different brain regions. Expression levels of the long form of aromatase were studied in the amygdala, BNST, POA, dorsal hippocampus, and cingulate cortex of castrated male, gonadally intact male, ovx female and ovx+E2 female rats. Each panel represents a different brain region. For each panel, qPCR amplification curves with relative fluorescent units (RFU) and the area punch dissected (red circle in the schematics of brain coronal sections, adapted from [48] ) are shown at the top. C T (cycle threshold) values on the amplification curve indicate the number of cycles required for the fluorescent signal to cross the threshold, which was set at 10 standard deviations above mean fluorescence generated during baseline cycles. Relative aromatase mRNA expression for each brain region is shown in bar graphs (ovx females set as 1.0) with representative images of agarose gels showing RT-PCR products for amplified aromatase (Aro) and GAPDH DNA fragments at the bottom. In the amygdala (A) , aromatase mRNA levels were affected by both sex (p = 0.006) and gonadal/hormonal status (p = 0.01), whereas in the BNST (B) and the POA (C) , gonadally intact males showed the highest aromatase mRNA expression, which was significantly different from all other groups; ** significant difference between intact males and other groups (p

    Journal: PLoS ONE

    Article Title: Quantitative Analysis of Long-Form Aromatase mRNA in the Male and Female Rat Brain

    doi: 10.1371/journal.pone.0100628

    Figure Lengend Snippet: Effect of gonadal/hormonal status on aromatase mRNA expression in different brain regions. Expression levels of the long form of aromatase were studied in the amygdala, BNST, POA, dorsal hippocampus, and cingulate cortex of castrated male, gonadally intact male, ovx female and ovx+E2 female rats. Each panel represents a different brain region. For each panel, qPCR amplification curves with relative fluorescent units (RFU) and the area punch dissected (red circle in the schematics of brain coronal sections, adapted from [48] ) are shown at the top. C T (cycle threshold) values on the amplification curve indicate the number of cycles required for the fluorescent signal to cross the threshold, which was set at 10 standard deviations above mean fluorescence generated during baseline cycles. Relative aromatase mRNA expression for each brain region is shown in bar graphs (ovx females set as 1.0) with representative images of agarose gels showing RT-PCR products for amplified aromatase (Aro) and GAPDH DNA fragments at the bottom. In the amygdala (A) , aromatase mRNA levels were affected by both sex (p = 0.006) and gonadal/hormonal status (p = 0.01), whereas in the BNST (B) and the POA (C) , gonadally intact males showed the highest aromatase mRNA expression, which was significantly different from all other groups; ** significant difference between intact males and other groups (p

    Article Snippet: The PCR reactions were prepared in triplicate in a 384-well plate by mixing 1.2 µl cDNA (10 µg) and 1.2 µl commercially available GoTaq qPCR master mix (Promega) using a Mosquito LCP automated liquid handler (TTP Labtech) and then adding 10 nl primer mix (for 200 nM of each primer in the final reaction) with an Echo Liquid Handler (Labcyte). qPCR was carried out using the following program: 95°C for 5 min, 40 cycles of 95°C for 15 sec and 60°C for 1 min, and a melt curve analysis (95°C for 15 sec, 60°C to 95°C with 0.5°C intervals, 30 sec per interval).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Amplification, Fluorescence, Generated, Reverse Transcription Polymerase Chain Reaction

    Programmed membrane protein (proMP) C2.1 asymmetric unit and structure statistics. Crystals of proMP C2.1 were obtained via lipid cubic phase (LCP) crystallization at 40 mg/ml peptide concentration as described in ‘Experimental methods.’ Screening was performed by the CSIRO Collaborative Crystallisation Centre (C3). Large rhomboid plates grown in 8% v/v 2-methyl-2,4-pentanediol, 0.1 M ADA (pH 6.7), 0.4 M potassium nitrate, 0.1 M tripotassium citrate were harvested and frozen in liquid nitrogen using 30% glycerol in precipitant solution as cryo-protectant. proMP C2.1 packs in the crystal as a trimer of dimers with two monoolein molecules (wheat stick representation) in the asymmetric unit. Purple ribbons and text represent the designed sequence; gray ribbons and text represent the appended N- and C-terminal sequences included to aid production and crystallization.

    Journal: eLife

    Article Title: De novo-designed transmembrane domains tune engineered receptor functions

    doi: 10.7554/eLife.75660

    Figure Lengend Snippet: Programmed membrane protein (proMP) C2.1 asymmetric unit and structure statistics. Crystals of proMP C2.1 were obtained via lipid cubic phase (LCP) crystallization at 40 mg/ml peptide concentration as described in ‘Experimental methods.’ Screening was performed by the CSIRO Collaborative Crystallisation Centre (C3). Large rhomboid plates grown in 8% v/v 2-methyl-2,4-pentanediol, 0.1 M ADA (pH 6.7), 0.4 M potassium nitrate, 0.1 M tripotassium citrate were harvested and frozen in liquid nitrogen using 30% glycerol in precipitant solution as cryo-protectant. proMP C2.1 packs in the crystal as a trimer of dimers with two monoolein molecules (wheat stick representation) in the asymmetric unit. Purple ribbons and text represent the designed sequence; gray ribbons and text represent the appended N- and C-terminal sequences included to aid production and crystallization.

    Article Snippet: For screening, LCP mixture was dispensed in 100 nl drops onto 96-well glass plates (Molecular Dimensions) with 1000 µl of precipitant solution using a Mosquito LCP robot (TTP Labtech) at RT.

    Techniques: Crystallization Assay, Concentration Assay, Sequencing

    Programmed membrane protein (proMP) 1.2 asymmetric unit and structure statistics. Crystals of proMP 1.2 were obtained via lipid cubic phase (LCP) crystallization at 35 mg/ml peptide concentration as described in ‘Experimental methods.’ Screening was performed by the CSIRO Collaborative Crystallisation Centre (C3). Oblong hexagonal discs grown in 25% w/v polyethylene glycol 1500, 10% v/v succinate-phosphate-glycine (pH 6.0) were harvested and frozen in liquid nitrogen using 30% glycerol in precipitant solution as cryo-protectant. proMP 1.2 packs in the crystal as a trimer (blue) with one monoolein molecule (wheat stick representation) and a less well-ordered helix that is antiparallel in orientation with respect to the trimer (light blue) in the asymmetric unit. Blue ribbons and text represent the designed sequence; gray ribbons and text represent the appended N- and C-terminal sequences included to aid production and crystallization.

    Journal: eLife

    Article Title: De novo-designed transmembrane domains tune engineered receptor functions

    doi: 10.7554/eLife.75660

    Figure Lengend Snippet: Programmed membrane protein (proMP) 1.2 asymmetric unit and structure statistics. Crystals of proMP 1.2 were obtained via lipid cubic phase (LCP) crystallization at 35 mg/ml peptide concentration as described in ‘Experimental methods.’ Screening was performed by the CSIRO Collaborative Crystallisation Centre (C3). Oblong hexagonal discs grown in 25% w/v polyethylene glycol 1500, 10% v/v succinate-phosphate-glycine (pH 6.0) were harvested and frozen in liquid nitrogen using 30% glycerol in precipitant solution as cryo-protectant. proMP 1.2 packs in the crystal as a trimer (blue) with one monoolein molecule (wheat stick representation) and a less well-ordered helix that is antiparallel in orientation with respect to the trimer (light blue) in the asymmetric unit. Blue ribbons and text represent the designed sequence; gray ribbons and text represent the appended N- and C-terminal sequences included to aid production and crystallization.

    Article Snippet: For screening, LCP mixture was dispensed in 100 nl drops onto 96-well glass plates (Molecular Dimensions) with 1000 µl of precipitant solution using a Mosquito LCP robot (TTP Labtech) at RT.

    Techniques: Crystallization Assay, Concentration Assay, Sequencing