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Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography
- Source :
- Star Protocols, STAR Protocols, STAR Protocols, Vol 3, Iss 1, Pp 101158-(2022)
- Publication Year :
- 2022
-
Abstract
- The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach. Finally, we cover data collection and structure determination using serial femtosecond crystallography. For complete details on the use and execution of this protocol, please refer to Durdagi et al. (2021).<br />Graphical abstract<br />The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach. Finally, we cover data collection and structure determination using serial femtosecond crystallography.
- Subjects :
- Models, Molecular
Science (General)
General Immunology and Microbiology
SARS-CoV-2
General Neuroscience
fungi
Crystallography, X-Ray
General Biochemistry, Genetics and Molecular Biology
body regions
Q1-390
X-ray Crystallography
X-Ray laser
Crystallography
Serials
Structural Biology
Protein Biochemistry
Protocol
Protein expression and purification
Humans
skin and connective tissue diseases
Protein biochemistry
Structural biology
X-ray crystallography
Crystallization
Coronavirus 3C Proteases
Subjects
Details
- ISSN :
- 26661667
- Volume :
- 3
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- STAR protocols
- Accession number :
- edsair.doi.dedup.....40cf803ccab9819dca767866929e0849