Glass Coaster : Protein crystal growth plate
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Protein crystal growth plate
Proteomics researcher holding a multi-well plate for growing protein crystals for X-ray crystallog- raphy studies. This is part of an automated system that can grow crystals faster than conventional methods. A solution of the protein being studied is placed in 480 wells, each with different conditions (acidity & salt concentration, for example). Crystals grow in the wells with the best conditions (which are unknown at the outset). The crystals are tiny, but are suitable for crystallo- graphy using the Advanced Light Source synchrotron at Lawrence Berkeley Labs, USA. The proteins str- ucture is determined from the diffraction pattern produced as X-rays pass through a crystal of it
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 6399519
© VOLKER STEGER/SCIENCE PHOTO LIBRARY
Analysis Crystal Crystallography Crystals Lawrence Berkeley Laboratory Plate Proteins Proteomics Researcher Sample Scientific Scientist Structural Tray Us A Bio Chemistry Biochemical Laboratory Protein
Glass Coaster
Individual Glass Coaster. Stylish and elegant polished safety glass, toughened and heat resistant (10x10cm, 7mm thick). Price shown is per individual coaster.
Individual Glass Coaster. Elegant polished safety toughened glass and heat resistant, matching Place Mats are also available
Estimated Image Size (if not cropped) is 7.6cm x 5.7cm (3" x 2.2")
Estimated Product Size is 10cm x 10cm (3.9" x 3.9")
These are individually made so all sizes are approximate
Artwork printed orientated as per the preview above, with landscape (horizontal) orientation to match the source image.
EDITORS COMMENTS
In this photo print, a dedicated proteomics researcher is seen holding a multi-well plate used for growing protein crystals. This cutting-edge automated system allows for faster crystal growth compared to traditional methods. The plate consists of 480 wells, each containing a different set of conditions such as acidity and salt concentration, which are crucial in determining the optimal environment for crystal formation. The true marvel lies in the unknown nature of these conditions at the beginning of the experiment. As proteins are carefully introduced into each well, tiny crystals begin to grow under ideal circumstances that remain concealed until later stages. These minuscule yet significant formations hold immense potential for X-ray crystallography studies conducted at Lawrence Berkeley Labs' Advanced Light Source synchrotron in the United States. By subjecting these protein crystals to X-rays and observing their diffraction patterns, scientists can unravel their intricate structures and gain valuable insights into their functions and behavior. This breakthrough technique opens up new avenues in biochemical analysis and structural biology. This awe-inspiring image encapsulates not only the scientific rigor but also highlights the dedication of female researchers like Mhairi Donohoe who tirelessly contribute to advancements in proteomics research. It serves as a testament to human ingenuity and our relentless pursuit of knowledge at esteemed institutions such as Lawrence Berkeley Laboratory (LBL).
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