Author: David N. Frick; Rajdeep S. Virdi; Nemanja Vuksanovic; Narayan Dahal; Nicholas R Silvaggi
Title: Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose Document date: 2020_4_2
ID: 02q9y011_17
Snippet: Crystallization and Structure Determination-In preparation for crystallization experiments, the purified SARS-CoV-2 macro X domain protein was cleaved with tobacco etch virus (TEV) protease to remove the N-terminal His6-tag and passed back through the Ni-NTA column. The flow-through fractions were desalted into 10 mM HEPES, pH 7.2 using a 2x5ml HiTrap desalting column (GE Life Sciences) and concentrated to 10 mg/mL in a centrifugal concentrator. .....
Document: Crystallization and Structure Determination-In preparation for crystallization experiments, the purified SARS-CoV-2 macro X domain protein was cleaved with tobacco etch virus (TEV) protease to remove the N-terminal His6-tag and passed back through the Ni-NTA column. The flow-through fractions were desalted into 10 mM HEPES, pH 7.2 using a 2x5ml HiTrap desalting column (GE Life Sciences) and concentrated to 10 mg/mL in a centrifugal concentrator. This preparation of the protein was mixed 1 μL:1 μL with the Morpheus HT screen reagents (Molecular Dimensions) in a 96-well SwissSci author/funder. All rights reserved. No reuse allowed without permission.
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