CSIRO Collaborative Crystallisation Centre (C3)

Australias only full service crystallisation centre


Dr. Janet Newman

You need to login or register to bookmark/favorite this content.

Post author: Shane Seabrook. Last update: 24/07/2015 at 4:42 pm by Gerard Gibbs.


The CSIRO Collaborative Crystallisation Centre (C3) is a full service protein crystallisation centre specialising in both screening and optimisation. Our mission is to provide both expert and novice users access to technologies which will enable the rapid and efficient sampling of crystallisation space, in order to streamline the process of obtaining biological insights from structural studies. Our core competency is high-throughput small volume (sub-microlitre) dispensing coupled with automatic imaging, but our strength lies in our ease of use, range of services and expert advice.

All sample booking and all images are available via secure web applications. We carry a large range (over 50) of commercial initial screens, as well as offering custom screen design and manufacture. We can provide high-throughput microseeding, along with additive screening or a combination of the two for optimisation of initial crystal hits. We provide novel tools for screen selection, sample volume calculators and batchload wizards to demystify the process of protein crystallogenesis. We run quality checks on all samples run through the CSIRO C3 and these are available through the C3 booking software. The experiments that are set up in the CSIRO C3 are available for downstream work – many crystals grown in C3 are suitable for analysis at the Australian Synchrotron without having to re-optimise in a larger format.

We hold regular user meetings where users are invited to give feedback about C3 and we use these to ensure that we are fulfilling the needs of the research community.  We also organise regular courses in crystallisation of macromolecules.

Other infrastructure:

  • C3 booking software.
  • C6 screen selection tool.
  • See3 data management tool.
  • Rigaku Crystaltrak database /CTweb tool with custom improvements.

Access by:

  • Research collaboration.
  • Fee for service.



The Collaborative Crystallisation Centre (C3) provides infrastructure to enable growth of the crystals which are required to obtain atomic-level protein structures via X-ray diffraction techniques.


Contact the facility manager or view our website for more information. We have web-based tools to allow our clients to book, view and optimise their experiments. This makes C3 accessible to local, national and international research groups.

Access by fee for service
Access by users external to managing organisation, Access by users internal to managing organisation


Dr. Janet Newman

Dr. Janet Newman

Facility Manager at CSIRO, Materials Science and Engineering Parkville Campus.

P: (03) 9662-7326 | Email |

Dr. Shane Seabrook

Dr. Shane Seabrook

Facility Staff at CSIRO, Materials Science and Engineering Parkville Campus.

Email |


Formulation Screening

Used for high-throughput screening of formulations to optimise protein stability..

Facility contact: |

Membrane Protein Crystallisation

Used for crystallisation screening of membrane proteins .

Facility contact: |

Nano Dispensing

Used for conducting smaller-scale experiments (10x less sample) than in a typical manual experiment..

Facility contact: |

Optimisation Screening

Used for completing combinatorial mixing from a wide range of stock solutions..

Facility contact: |


CSIRO Collaborative Crystallisation Centre (C3)

CSIRO, Materials Science and Engineering Parkville Campus. 388 Royal Parade, Parkville, Victoria, Australia.

View location in Google maps.


Type: Core facility in a research organisation
Discipline areas: Biological Science
Precinct: Central
Affiliations: CSIRO
Accreditation: ISO 17025
Biological Science categories: Computational, Crystallisation, Data storage, Properties and interactions, Proteins and peptides, Structural biology, X-ray crystallography and SAXS

Tags: Crystallisation, Crystallization, Protein, Protein Function, Protein Stability, Protein Structure, Structural Biology