Framed Print : EcoRV restriction enzyme molecule C014 / 2114
Framed Photos from Science Photo Library
EcoRV restriction enzyme molecule C014 / 2114
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (white and gold) bound to a cleaved section of DNA (deoxyribonucleic acid, orange and yellow). Restriction enzymes, also known as restriction endonucleases, recognise specific nucleotide sequences and cut the DNA at these sites. They are found in bacteria and archaea and are though to have evolved as a defence against viral infection. Type II restriction enzymes cut double stranded DNA. EcoRV is found in some strains of Escherichia coli bacteria. This structure is based on X-ray crystallography data
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 9261887
© RAMON ANDRADE 3DCIENCIA/SCIENCE PHOTO LIBRARY
1rvc Asymmetric Unit Bacterial Bacteriology Cleaved Crystallography Deoxyribonucleases Dimer Complex E Coli Eco321 Ecorv Enzyme Escherichia Coli Homodimer Microbiology Molecular Biology Restriction Fragment Secondary Structure Site Specific Type Ii Type Ii Restriction Endonuclease Biochemical Biochemistry Cutouts Deoxyribonucleic Acid Genetics Microbiological Molecular Molecular Model Protein
12"x10" Modern Frame
Introducing the Media Storehouse Framed Prints featuring the captivating 3D molecular model of EcoRV restriction enzyme by Ramon Andrade from Science Photo Library. Witness the intricate interaction between the white and gold EcoRV enzyme and the orange and yellow cleaved section of DNA in high resolution. This stunning representation of the type II restriction enzyme's binding to DNA is a must-have for any lab, classroom, or office space. Embrace the beauty of science with our expertly crafted and beautifully framed prints.
10x8 Print in an MDF Wooden Frame with 180 gsm Satin Finish Paper. Glazed using shatter proof thin plexi glass. Frame thickness is 1 inch and depth 0.75 inch. Fluted cardboard backing held with clips. Supplied ready to hang with sawtooth hanger and rubber bumpers. Spot clean with a damp cloth. Packaged foam wrapped in a card.
Contemporary Framed and Mounted Prints - Professionally Made and Ready to Hang
Estimated Image Size (if not cropped) is 25.4cm x 25.4cm (10" x 10")
Estimated Product Size is 25.4cm x 30.5cm (10" x 12")
These are individually made so all sizes are approximate
Artwork printed orientated as per the preview above, with landscape (horizontal) or portrait (vertical) orientation to match the source image.
EDITORS COMMENTS
This print showcases the EcoRV restriction enzyme molecule C014/2114, a type II restriction enzyme found in certain strains of Escherichia coli bacteria. The molecular model of this enzyme is depicted in white and gold, while the cleaved section of DNA it is bound to appears in vibrant shades of orange and yellow. Restriction enzymes, also known as restriction endonucleases, play a crucial role in genetic defense mechanisms against viral infections. They possess the remarkable ability to recognize specific nucleotide sequences within DNA and cut the double-stranded molecule at these precise sites. This particular structure is based on X-ray crystallography data, providing an accurate representation of its intricate details. The image highlights the significance of EcoRV as a homodimeric protein involved in site-specific DNA cleavage. Its presence within bacterial and archaeal cells underscores its evolutionary importance for protection against viral invasion. Displayed against a clean white background, this artwork beautifully captures the complex nature of molecular biology and biochemistry. It serves as a visual reminder of the fascinating world that exists at microscopic levels – where proteins interact with DNA to shape life's building blocks. This stunning print by RAMON ANDRADE 3DCIENCIA/SCIENCE PHOTO LIBRARY offers both scientific insight and aesthetic appeal for those interested in microbiology, genetics, or simply appreciating the wonders hidden within our biological systems.
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