Equipment and services
Outstanding facilities and equipment are critical to BIC’s mission of delivering world-class research in biomolecular interactions at the interface of engineering and science. As such, BIC continues to invest strategically in capital equipment and in its ongoing maintenance.
We have a range of advanced technologies to enhance our ability to study biomolecular interactions. If you are interested in learning about or using any of the facilities below, please use our equipment and services booking form.
The New Zealand Analytical Ultracentrifugation Centre (NZAUC) is the only centre of its kind in New Zealand. The analytical ultracentrifuge allows researchers to probe the molecular mass of biomolecules in solution and to characterise interactions between different biomolecules (e.g. protein-DNA interactions).
Developments in instrumentation and data analysis have greatly increased the potential of the facility to deal with complicated systems, including inorganic crystalline nanoparticles and interactions within cell lysates and food, and to provide information complementary to other techniques, such as surface plasmon resonance (SPR).
The AUC is accessible to outside organisations on a contract or collaborative basis. For more information contact email@example.com.
An automated analysis used for size and quantitation analysis of protiens, DNA and RNA. It works through microfluidic separation that produces size and electropherogram results for quantitative analysis from pure samples to cell lysates.
Within the BIC we have a range of biomolecule purification equipment, including various AKTA systems (Pure, Basic and Express systems) and associated columns and media for any type of purification. We also have detection systems for absorbance and fluorescence.
Circular Dichroism allows the determination of protein secondary and tertiary structure. It can also be used to evaluate DNA quadruplex structure. It is often used to determine the chemical or temperature stability of biomolecules.
A confocal microscope detects the fluorescence emitted when the specimen is scanned by a laser, resulting in high-resolution images and the ability to directly observe dynamic processes in live cells. Cell components can be precisely localised, and accurate three-dimensional information is easily obtained. The behaviour and interactions of molecules can be studied.
Our inverted Leica TCS SP5 confocal microscope is equipped with a full range of lasers from 405nm to 633nm, as well as incubation and heating/cooling chambers.
The confocal microscope is accessible to outside organisations on a contract or collaborative basis.
For more information see Leica's website.
Determine protein folding, domain structure and the effect of solution conditions of mutations, ligand binding and chemical labelling on protein conformation.
A dynamic light scattering system for particle and molecular weight measurements. Analysing protein charge and iso-electric point through pH titration, interactions of protein aggregation and oligomerisation state and protein-protein binding in a range of solvents, measurements of colloid and emulsion solutions.
This system is able to measure the presence of his-tagged protein or analyse binding kinetics. Results are very quick. You can view binding events in real time, measure kinetic rates for association, dissociation and affinity. Assays require only 4 ul of sample, and can be performed in complex mixtures, or even crude solutions.
BIC recently purchased a Dionex ICS 5000: a high-performance anion exchange chromatography system. This analytical facility allows the high-resolution analysis and separation of anions. The detector system used is electrochemical (pulsed amperometric detection, PAD, sometimes also called pulsed electrochemical detection, PED), and is extremely sensitive; significantly more so than typical HPLC detectors.
A wide variety of different columns are available for use with the system, which allow a very broad range of analytical applications.
In addition to anions, as the eluent used is sodium hydroxide, weakly acidic organic compounds, such as reducing sugars are also very amenable to analysis. The ICS system is capable of mono-, oligo- and polysaccharide analysis and profiling, and finds applications in disciplines as disparate as Glycobiology and Food Science.
This instrument is accessible to outside organisations. It requires the purchase of specific columns and eluent.
The interaction between molecules often accompanies a change in thermal energy. ITC quantifies this change allowing the precise determination of the thermodynamics of a biomolecular interaction. It is useful for protein-protein, protein-peptide, protein-ligand and protein-small molecule interactions.
Determines protein folding, domain structure and the effect of solution conditions of mutations, ligand binding and chemical labelling on protein conformation.
The NanoLab contains facilities for semiconductor material processing, nanofabrication, and sensor and microfluidic device development.
The equipment covers most aspects of semiconductor device fabrication, from materials growth and characterisation to device packaging. The principal tools are:
- Atomic Force Microscope (Digital Instruments Dimension 3100)
- Deep Reactive Ion Etching (Oxford PlasmaPro 100 Cobra)
- Electron Beam Lithography (Raith 150)
- Interference Lithography
- Mask Writing (Heidelberg uPG101)
- Micromilling (CNC Mini- Mill/GX)
- Nanoimprint Lithography (EVG)
- Optical Lithography (Suss MA-6)
- Optical Microscopy (Olympus BX30 with digital image capture)
- Plasma Ashing (Tergeo plasma cleaner)
- Semiconductor Device Characterisation (HP 4155A Parameter Analyser)
- Surface Profilometer (Profilm3D)
- Thin Film Deposition (Edwards AUTO 500, Temescal FC-1800 and Mist CVD)
- Wire Bonding (Kulicke & Soffa 4500)
The facility is accessible to external organisations on a contract or collaborative basis.
Equipped with a Fluorescence and Florescence anisotropy detector and heating to 60 degrees.
The BIC has a Mosquito protein crystallography robot that allows us to setup crystallisation trials easily and effectively. The drop sizes are usually 200-400 nL and the usual setup is a 96 well plate.
Purchased in 2016, this instrument supports the growing number of structural biology projects within BIC. In addition to real-time polymerase chain reactions (PCR), the instrument also offers rapid and simple protein stability screens by thermal melts.
It combines a thermal cycler and optical reaction module for singleplex and multiplex detection of fluorophores. The system features thermal gradient functionality and automation capabilities.
Scattering of visible light can be used to determine the size and overall dimensions of macromolecules in solution. Absolute molecular weight can then be calculated directly from the light scatter, but this requires accurate measurement of protein concentration. To achieve this the Viscotek has detectors for refractive index and UV. Additionally, the Viscotek has a viscometer, which allows determination of molecular size, conformation, and structure.
Determines the size and structural characterisation of molecules in solution. Detector functions include low angle light scattering, right angle light scattering, viscometer and refractive index.
Uses an optical detection process called surface plasmon resonance which can analyse up to 36 different protein, peptide, DNA and small molecule interactions in a single run. Measures different experimental conditions including kinetics.
Utilised to monitor the speed of biomolecular reactions. Equipped with multicell block and temperature control.