ACRF Biomolecular Resource Facility

Terms and Policies

1) The BRF operates on a cost recovery, the percentage of which is determined by the School.

2) No samples/orders will be processed without an authorised sample submission/order form and valid charge code.

3) It is a condition of the contract between the ACRF and JCSMR/ANU that "the Foundation (ACRF) is to be acknowledged in all scientific publications which utilise the Facility (BRF) at the Institute (JCSMR)".

All work performed in the BRF, whether full service or not, and the use of any BRF resources should be acknowledged in all publications arising from that work. This should be in the “Material and Methods” section of the paper (see examples below). Any further individual acknowledgements are solely at your discretion.

4) A reference to the publication should be sent to the Manager of the BRF once the paper is published (includes theses).

5) BRF collaborations and co-authorship: Although the BRF is primarily a service unit, there are instances where BRF staff make significant contributions to either the technical or intellectual input of the project. This should be discussed with the staff member concerned prior to commencement of the collaboration.

Examples:
Real-time PCR
Amplifications were performed in 384-well optical reaction plates (Applied Biosystems) with a 7900HT Fast Real-Time PCR System (at the ACRF Biomolecular Resource Facility, JCSMR, ANU) using SDS 2.2.2 software to analyse raw data.

DNA Sequencing
Amplified PCR products were agarose gel purified and sequenced on an ABI 3730 sequencer (ACRF Biomolecular Resource Facility, JCSMR, ANU) following the manufacturer's protocol (Applied Biosystems 2002).

Peptide synthesis
Peptides were synthesized chemically using the 9-fluorenylmethyl-oxycarbonyl (FMOC) method on a Rainen Symphony/Multiplex peptide synthesizer, and supplied by the ACRF Biomolecular Resource Facility at the John Curtin School of Medical Research, Australian National University. As required, the N- or C-terminus, or both, were protected by acetylation or amidation, respectively.

Tetramer synthesis
Cells were surface stained with APC-labelled tetramers consisting of murine class I MHC molecule (H-2Db), b2-microglobulin and influenza nucleoprotein peptide NP366–374. Tetramers were synthesised in the ACRF Biomolecular Resource Facility at The John Curtin School of Medical Research, using BirA enzyme synthesized as described (O’Callaghan et al., 1999).
[O’Callaghan, C.A., Byford, M.F., Wyer, J.R., Willcox, B.E., Jakobsen, B.K., McMichael, A.J. and Bell, J.I (1999). BirA Enzyme: Production and Application in the study of membrane receptor-ligand interactions by site-specific biotinylation. Anal. Biochem. 266, 9-15.]