Journal: PLoS ONE

Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin

doi: 10.1371/journal.pone.0050161

Figure Lengend Snippet: The figure shows a sequence alignment of domains of Drosophila and human spastin, as well as human katanin. The black contour highlights the position of the human spastin linker, residues with a high degree of conservation are red, residues with low degree are blue. The location of the highly basic patch in human spastin is boxed in blue. Above the alignment, the location of the sequence in the context of human spastin is indicated, below the location in human katanin. For details, see text.

Article Snippet: A codon-optimized version of full-length human katanin was synthesized commercially (MorphoSys/Sloning; Planegg, Germany).

Techniques: Sequencing

Journal: PLoS ONE

Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin

doi: 10.1371/journal.pone.0050161

Figure Lengend Snippet: Nucleotide dependence of microtubule interaction.

Article Snippet: A codon-optimized version of full-length human katanin was synthesized commercially (MorphoSys/Sloning; Planegg, Germany).

Techniques:

Journal: PLoS ONE

Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin

doi: 10.1371/journal.pone.0050161

Figure Lengend Snippet: Salt dependence of microtubule interaction.

Article Snippet: A codon-optimized version of full-length human katanin was synthesized commercially (MorphoSys/Sloning; Planegg, Germany).

Techniques:

Journal: PLoS ONE

Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin

doi: 10.1371/journal.pone.0050161

Figure Lengend Snippet: Panel A displays the constructs used for katanin binding experiments. Panel B shows a quantitative SDS-gel of supernatants (unbound) and pellets (microtubule-bound) of an in vitro binding assay of truncated katanin constructs and microtubules. Increasing microtubule concentrations (0 to 10 µM) were incubated with a fixed katanin construct concentration (1 µM). The density of the katanin construct band was plotted against the microtubule concentration and fitted to a Hill function (panel C). The half-maximal saturation was reached at 0.34 µM (Kat12) and 0.40 µM (Kat2). Only constructs containing domain 2 were able to bind to microtubules.

Article Snippet: A codon-optimized version of full-length human katanin was synthesized commercially (MorphoSys/Sloning; Planegg, Germany).

Techniques: Construct, Binding Assay, SDS-Gel, In Vitro, Incubation, Concentration Assay

Journal: PLoS ONE

Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin

doi: 10.1371/journal.pone.0050161

Figure Lengend Snippet: Binding stoichiometry.

Article Snippet: A codon-optimized version of full-length human katanin was synthesized commercially (MorphoSys/Sloning; Planegg, Germany).

Techniques: Binding Assay

Journal: PLoS ONE

Article Title: Spastin's Microtubule-Binding Properties and Comparison to Katanin

doi: 10.1371/journal.pone.0050161

Figure Lengend Snippet: Panel A shows a SDS-gel of co-sedimentation assays with katanin (E309Q mutant, 1 mM ATP) and a constant concentration of microtubules (2 µM; indicated by a dotted line). With increasing katanin concentrations, an increasing amount of protein is co-sedimented with microtubules. Panel B: Plot of the densitometric analysis as in . Panel C shows the same experiment for wild type katanin.

Article Snippet: A codon-optimized version of full-length human katanin was synthesized commercially (MorphoSys/Sloning; Planegg, Germany).

Techniques: SDS-Gel, Sedimentation, Mutagenesis, Concentration Assay

Journal: Methods in cell biology

Article Title: Heterologous expression of plant glycosyltransferases for biochemistry and structural biology

doi: 10.1016/bs.mcb.2020.05.002

Figure Lengend Snippet: List of primers used to amplify genes in this study.

Article Snippet: In this example, a codon optimized version of the full-length ORF of XLT2 (henceforth referred to as OptXLT2) was synthesized by a commercial supplier (GenScript) using their in-house codon optimization parameters and used as a PCR template to generate different truncation variants.

Techniques: Sequencing

Journal: PLoS ONE

Article Title: Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

doi: 10.1371/journal.pone.0112555

Figure Lengend Snippet: Table 2. Cry35Ab1 (4JP0) data processing, model and refinement statistics.

Article Snippet: A transgenic corn line encoding full length versions of both Cry34Ab1and Cry35Ab1 was jointly developed by Dow AgroSciences and Pioneer Hi-Bred International , and sold under the brand name HERCULEX RW.

Techniques:

Journal: PLoS ONE

Article Title: Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

doi: 10.1371/journal.pone.0112555

Figure Lengend Snippet: (A) The structure of Cry34Ab1 is a β-sandwich of 10 strands. (B) Cry35Ab1 contains two domains. The N-terminal trefoil domain contains α-helices and three β-sheets. The C-terminal domain is terminated with a three helix fold which is not required for activity . This figure, and all subsequent structure representations, were made with PyMOL .

Article Snippet: A transgenic corn line encoding full length versions of both Cry34Ab1and Cry35Ab1 was jointly developed by Dow AgroSciences and Pioneer Hi-Bred International , and sold under the brand name HERCULEX RW.

Techniques: Activity Assay

Journal: PLoS ONE

Article Title: Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

doi: 10.1371/journal.pone.0112555

Figure Lengend Snippet: (A) The SAXS calculated envelope of Cry34 matches closely to the crystal structure. The top view is related to the bottom view by 90° rotation to the bottom of the page. (B) The trCry35Ab1 SAXS structures are in good agreement with the Cry35Ab1 crystal structure. No higher order structures or oligomeric states were evident in either the Cry34Ab1 or trCry35Ab1 SAXS data. It is clear that both toxins are monomeric in solution in the absence of a receptor or binding partner.

Article Snippet: A transgenic corn line encoding full length versions of both Cry34Ab1and Cry35Ab1 was jointly developed by Dow AgroSciences and Pioneer Hi-Bred International , and sold under the brand name HERCULEX RW.

Techniques: Binding Assay

Journal: PLoS ONE

Article Title: Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

doi: 10.1371/journal.pone.0112555

Figure Lengend Snippet: Table 5. Combinatorial extension analysis of PDB submitted structures against Cry35Ab1 coordinates.

Article Snippet: A transgenic corn line encoding full length versions of both Cry34Ab1and Cry35Ab1 was jointly developed by Dow AgroSciences and Pioneer Hi-Bred International , and sold under the brand name HERCULEX RW.

Techniques: Binding Assay

Journal: PLoS ONE

Article Title: Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

doi: 10.1371/journal.pone.0112555

Figure Lengend Snippet: (A) Overlay of the Cry34Ab1 structure (purple) with a model of Pam (green). (B) Overlay of the Cry35Ab1 crystal structure (blue) with a model of Cry49 (green). See text for details.

Article Snippet: A transgenic corn line encoding full length versions of both Cry34Ab1and Cry35Ab1 was jointly developed by Dow AgroSciences and Pioneer Hi-Bred International , and sold under the brand name HERCULEX RW.

Techniques:

Journal: PLoS ONE

Article Title: Structural and Biophysical Characterization of Bacillus thuringiensis Insecticidal Proteins Cry34Ab1 and Cry35Ab1

doi: 10.1371/journal.pone.0112555

Figure Lengend Snippet: Cry35Ab1 is structurally related to a wide variety pore-forming proteins as assessed by combinatorial extension. All structures contain a conserved beta-sheet core and varying loop regions.

Article Snippet: A transgenic corn line encoding full length versions of both Cry34Ab1and Cry35Ab1 was jointly developed by Dow AgroSciences and Pioneer Hi-Bred International , and sold under the brand name HERCULEX RW.

Techniques: