Corporate Banner
Satellite Banner
Crystallography
Scientific Community
 
Become a Member | Sign in
Home>News>This Article
  News
Return

Understanding Protein Crystallization Growth at the University of Leeds Using a Temperature Stage

Published: Wednesday, June 27, 2012
Last Updated: Wednesday, June 27, 2012
Bookmark and Share
LTS350 hot-stage system used to visualize and grow HEW lysozyme crystals.

Linkam Scientific Instruments report on the use of their LTS350 stage at the University of Leeds to visualize and grow HEW lysozyme crystals.

The Institute for Particle Science and Engineering is a centre of excellence within the School of Process, Environmental and Materials Engineering at the University of Leeds.

Researchers here focus on projects that address the engineering science of particulate processes and products. PhD and MSc students have been using an LTS350 hot-stage system in their research for several years.

Currently, Research Fellow, Dr Jingjing Liu is using the stage in her experiments to study how protein crystallization is affected by growing the crystals in a larger quantity, and by changing the cooling rate.

Traditional methods for growing protein crystals are by micro plate sitting-drop crystallization, or by hanging-drop methods based on vapour diffusion. These methods yield a limited number of crystals but in biological research this is usually enough.

Each of the stages within the LTS range are well-suited to studying protein crystallization. These versatile heating and freezing stages consist of a large area temperature controlled element with a platinum temperature sensor embedded close to the surface for accurate measurements.

The LTS stage has the facility to heat sufficient amounts of liquid within a crucible, which comes with a lid to prevent evaporation. The LTS350 system has now been replaced by the LTS420 which has the same features but has an expanded temperature range of -196°-420°C.

Dr Liu is using HEW lysozyme (Hen Egg-White lysozyme) and is trying to observe the behaviour of protein crystals within a population. To grow a population she uses a quartz crucible to crystallize them inside the LTS350 hot-stage.

The number of crystals is proportional to the amount of liquid used within the crucible. The relatively large capacity of the quartz crucible is a distinct benefit in this research as Dr Liu can grow the HEW lysozyme crystals in a useful quantity.

In addition the whole process of protein crystallization can be recorded by a video/camera system.

She can also run experiments for over twelve hours, other systems prohibit such long experiments as the liquid can evaporate in the crucible.

Lysozyme forms part of the innate immune system of a wide number of organisms including mammals, and as a result is significant in the onset and control of disease.

Hen egg-white lysozyme has been extensively studied and is the first enzyme structure to be solved by X-ray diffraction methods and first enzyme to be fully sequenced that contains all twenty common amino acids.

Lysozyme hydrolyzes the beta-glycosidic linkage between N-acetylmuramic acid and N-acetyl glucosamine in the peptidoglycan of bacterial cell walls. Under a variety of conditions it has a consistent structure, making it ideal for crystallography studies.

Protein crystals have shown significant benefits in the delivery of biopharmaceuticals but the majority (with a few exceptions such as insulin) are not yet marketed in this way. Historically the work in this field is, Dr Liu says: "focused on investigations on crystal growth looking at the molecular and single crystal scales."

She notes that this differs from her research as: "my research is focused on understanding the growth behaviour of the population of crystals which is clearly important to mass crystal growth."


Further Information
Access to this exclusive content is for Technology Networks Premium members only.

Join Technology Networks Premium for free access to:

  • Exclusive articles
  • Presentations from international conferences
  • Over 2,500+ scientific posters on ePosters
  • More than 3,700+ scientific videos on LabTube
  • 35 community eNewsletters


Sign In



Forgotten your details? Click Here
If you are not a member you can join here

*Please note: By logging into TechnologyNetworks.com you agree to accept the use of cookies. To find out more about the cookies we use and how to delete them, see our privacy policy.

Related Content

Temperature Controlled Stage Used in Crystallisation Processes
Linkam Scientific Instrument report on the work of Professor Yves Henri Geerts from the Université Libre de Bruxelles where he uses a specially designed temperature stage to study crystallisation processes in opto-electronic thin films.
Friday, December 09, 2011
Scientific News
Structural Discoveries Could Aid in Better Drug Design
Scientists have uncovered the structural details of how some proteins interact to turn two different signals into a single integrated output.
New Mathematics Advances the Frontier of Macromolecular Imaging
Berkeley Lab’s M-TIP solves the reconstruction problem for fluctuation X-ray scattering.
Diamond Helps Develop New Way of Studying the Tiniest Microcrystals
Researchers have developed a new type of sample holder for ‘serial protein crystallography’.
Crystal Clear Images Uncover Secrets of Hormone Receptors
NIH researchers gain better understanding of how neuropeptide hormones trigger chemical reactions in cells.
TOPLESS Plants Provide Clues to Human Molecular Interactions
Scientists at Van Andel Research Institute have revealed an important molecular mechanism in plants that has significant similarities to certain signaling mechanisms in humans, which are closely linked to early embryonic development and to diseases such as cancer.
Advancing Cancer Drug Design with Image of Key Protein
Scientists have pioneered the use of a high-powered imaging technique to picture in exquisite detail one of the central proteins of life – a cellular recycling unit with a role in many diseases.
Mould Unlocks New Route to Biofuels
Scientists at The University of Manchester have made an important discovery that forms the basis for the development of new applications in biofuels and the sustainable manufacturing of chemicals.
'Invisible' Protein Structure Explains the Power of Enzymes
A research group at Umeå University in Sweden has managed to capture and describe a protein structure that, until now, has been impossible to study.
Unraveling the Elusive Structure of HIV Protein
Snapshots of HIV virus’ proteins may help design new ways to fight the disease.
Blueprinting Cell Membrane Proteins
Recent breakthrough will make the blueprinting process faster, easier and cheaper, and should have major implications in the field of drug discovery and development.
Skyscraper Banner

Skyscraper Banner
Go to LabTube
Go to eposters
 
Access to the latest scientific news
Exclusive articles
Upload and share your posters on ePosters
Latest presentations and webinars
View a library of 1,800+ scientific and medical posters
2,500+ scientific and medical posters
A library of 2,500+ scientific videos on LabTube
3,700+ scientific videos
Close
Premium CrownJOIN TECHNOLOGY NETWORKS PREMIUM FREE!