3CLpro C145S was incubated overnight with a 0.01-fold molar ratio of Human NEMO capped peptide and incubated overnight at 4 °C. No precipitation was observed. TOP96 (Rigaku Reagents, Japan), BCS (Molecular Dimensions, UK) and GRAS2 (Hampton Research, USA) screens were run using a Gryphon (Art Robbins Instruments, USA). 0.2 μL of protein solution at 6.5 mg/mL was added to 0.2 μL of crystallization matrix in a sitting-drop vapor diffusion setup at 18 °C. BCS screen condition A9 (0.1 M MES pH 6.5, 20 % v/v PEG Smear High) produced needle-like crystal clusters of 3CLpro C145S.
Gras2
Manufactured by Hampton Research
Sourced in United Kingdom
GRAS2 is a laboratory instrument designed for the rapid and efficient analysis of gas samples. The core function of GRAS2 is to provide precise and accurate measurements of the composition and properties of various gas mixtures. This instrument utilizes advanced analytical techniques to deliver reliable data for research and industrial applications.
Automatically generated - may contain errors
Lab products found in correlation
3 protocols using gras2
1
Structural Analysis of 3CLpro C145S Mutant
2
Crystallization of 3CLpro C145S-Nemo Complex
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Human NEMO capped peptide (residues 226-235, acetyl-KLAQLQVAYH-amide, synthesized by Thermo Scientific) was dissolved to 2 mM in peptide buffer (20 mM HEPES, 150 mM NaCl, pH 7.2) and DMSO (5.67%). Peptides were then added to 3CLpro C145S at a 20-fold molar excess, before overnight incubation at 4 °C. The mixture was centrifuged to remove precipitants, and the supernatant was concentrated to 6.5 mg/mL for crystallization screens.
TOP96 (Rigaku Reagents, Japan), BCS (Molecular Dimensions, UK) and GRAS2 (Hampton Research, USA) screens were run using a Gryphon (Art Robbins Instruments, USA). 0.2 µL of protein solution at 6.5 mg/mL was added to 0.2 µL of crystallization matrix in a sitting-drop vapor diffusion setup at 18C. GRAS2 screen condition F11 (0.1 M Sodium phosphate dibasic dihydrate, pH 9.3, 10 mM Calcium chloride, 20% w/v Polyethylene glycol 3,350), yielded platelike single crystals. These crystals were isolated, cryoprotected by supplementation with 20% glycerol, mounted into ALS style, 0.05-0.1 mm loops (Hampton Research, USA) and flash frozen in liquid nitrogen.
TOP96 (Rigaku Reagents, Japan), BCS (Molecular Dimensions, UK) and GRAS2 (Hampton Research, USA) screens were run using a Gryphon (Art Robbins Instruments, USA). 0.2 µL of protein solution at 6.5 mg/mL was added to 0.2 µL of crystallization matrix in a sitting-drop vapor diffusion setup at 18C. GRAS2 screen condition F11 (0.1 M Sodium phosphate dibasic dihydrate, pH 9.3, 10 mM Calcium chloride, 20% w/v Polyethylene glycol 3,350), yielded platelike single crystals. These crystals were isolated, cryoprotected by supplementation with 20% glycerol, mounted into ALS style, 0.05-0.1 mm loops (Hampton Research, USA) and flash frozen in liquid nitrogen.
3
Crystallization of Protein Complexes
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TOP96 (Rigaku Reagents, Japan), BCS (Molecular Dimensions, UK) and GRAS2 (Hampton Research, USA) screens were run using a Gryphon (Art Robbins Instruments, USA). 0.2 μL of protein solution at 6.5 mg/mL was added to 0.2 μL of crystallization matrix in a sitting-drop vapor diffusion setup at 18 °C. GRAS2 screen condition F11 (0.1 M Sodium phosphate dibasic dihydrate, pH 9.3, 10 mM Calcium chloride, 20% w/v Polyethylene glycol 3,350), yielded platelike single crystals. These crystals were isolated, cryoprotected by supplementation with 20% glycerol, mounted into ALS style, 0.05–0.1 mm loops (Hampton Research, USA) and flash frozen in liquid nitrogen.
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