Source 1primary paper2019
Toolkit/AcrIIC3-LOV2 light-switchable anti-CRISPR hybrid
AcrIIC3-LOV2 light-switchable anti-CRISPR hybrid
Also known as: AcrIIC3-LOV2 hybrids, engineered, light-dependent anti-CRISPR protein
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
AcrIIC3-LOV2 is an engineered light-switchable anti-CRISPR protein formed by fusing the Neisseria meningitidis Cas9 inhibitor AcrIIC3 to the Avena sativa LOV2 blue-light sensory domain. In mammalian cells, two reported hybrids strongly inhibit NmeCas9 in the dark and allow robust genome editing under blue-light irradiation.
Usefulness & Problems
Why this is useful
This tool enables optogenetic control of NmeCas9 genome editing by coupling anti-CRISPR inhibition to blue light. It is useful for experiments requiring reversible, light-gated suppression of a type II-C CRISPR effector rather than constitutive Cas9 activity.
Problem solved
It addresses the problem of controlling NmeCas9 activity with temporal precision in mammalian cells. Specifically, it provides a way to keep NmeCas9 strongly inhibited in the dark while permitting editing after blue-light exposure.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Target processes
editingrecombinationInput: Light
Implementation Constraints
The construct is a fusion between AcrIIC3 and the Avena sativa LOV2 blue-light sensory domain. Reported function involves blue-light irradiation and was demonstrated in mammalian cells for control of NmeCas9 genome editing; no additional construct architecture, delivery method, or cofactor requirements are specified in the supplied evidence.
The supplied evidence is limited to two reported hybrids and mammalian-cell genome editing with NmeCas9. No independent replication, quantitative performance metrics, or validation in other CRISPR systems, organisms, or application contexts are provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c2 during normalization. Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation. Derived from claim c2. Quoted text: Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
Supporting Sources
Source 2primary paper2020Nucleic Acids Research
Ranked Claims
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
Approval Evidence
2 sources9 linked approval claimsfirst-pass slug acriic3-lov2-light-switchable-anti-crispr-hybrid
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
Source:
we created hybrids between the Nme Cas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
Source:
activity controlsupports
Two AcrIIC3-LOV2 hybrids potently blocked NmeCas9 activity in the dark while permitting robust genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked NmeCas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
design implicationsupports
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
Source:
engineering designsupports
The authors created hybrids between AcrIIC3 and the Avena sativa LOV2 blue light sensory domain.
we created hybrids between the NmeCas9 inhibitor AcrIIC3 and the LOV2 blue light sensory domain from Avena sativa
Source:
first reportsupports
This paper reports the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control NmeCas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
Source:
structural observationsupports
Structural analysis indicated that the LOV2 domain in the hybrids is located close to the Cas9 binding surface.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Source:
activity controlsupports
Two AcrIIC3-LOV2 hybrids blocked Nme Cas9 activity in the dark and permitted genome editing upon blue light irradiation.
Two AcrIIC3-LOV2 hybrids from our collection potently blocked Nme Cas9 activity in the dark, while permitting robust genome editing at various endogenous loci upon blue light irradiation.
Source:
design implicationsupports
The work demonstrates optogenetic regulation of a type II-C CRISPR effector and suggests a route for designing optogenetic anti-CRISPR proteins.
Together, our work demonstrates optogenetic regulation of a type II-C CRISPR effector and might suggest a new route for the design of optogenetic Acrs.
Source:
structural observationsupports
Structural analysis placed the LOV2 domain in close proximity to the Cas9 binding surface within the hybrids.
Structural analysis revealed that, within these hybrids, the LOV2 domain is located in striking proximity to the Cas9 binding surface.
Source:
tool introductionsupports
This work reports an optogenetic tool that controls Nme Cas9 activity in mammalian cells using an engineered light-dependent anti-CRISPR protein.
Here, we report the first optogenetic tool to control Nme Cas9 activity in mammalian cells via an engineered, light-dependent anti-CRISPR (Acr) protein.
Source:
Comparisons
Source-backed strengths
The reported hybrids potently blocked NmeCas9 activity in the dark and permitted robust genome editing upon blue-light irradiation. The study also demonstrated optogenetic regulation of a type II-C CRISPR effector, establishing a design route for light-switchable anti-CRISPR proteins.
Ranked Citations
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