Bruker Daltonics Introduces Novel Protein Post-Translational Modification -PTM- Discovery Tool on HCTultra Ion Trap.

BILLERICA, Mass. -- Bruker Daltonics Inc.

--First Commercial Availability of ETD Fragmentation Offers Unique Capabilities for PTM Discovery and De Novo Peptide Sequencing on High-Capacity Ion Traps

Bruker Daltonics Inc. today announces a commercial Electron Transfer Dissociation (ETD) module for its top-of-the-line high-capacity ion trap mass spectrometer, the HCTultra(TM). ETD is a unique new peptide and protein fragmentation technique that preserves functionally important post-translational modifications (PTMs), such as phosphorylation or glycosylation. With ETD in a high-capacity ion trap, protein scientists can sequence peptides easily, and in addition they can simultaneously identify both the type and location of various PTMs.

Dr. Detlev Suckau, Head of Proteomics Applications Development at Bruker Daltonics, commented: "Modern proteomics has moved beyond simple identification, and one of the primary goals of functional proteomics is now the unraveling of the many subtle modifications arising in proteins which often are very important for their biological activity. By making ETD capabilities available broadly to all protein scientists for specific PTM analyses on the ultra-high performance HCTultra ion trap, we continue our leadership in the area of top-down proteomics, where we have previously pioneered important related developments such as highest-performance commercial ECD on our FTMS, and our unique T3-sequencing on the Ultraflex TOF/TOF."

ETD MS/MS spectra of peptides can now be collected on-the-fly during LC/MS/MS runs using the HCTultra. Due to its non-ergodic nature, ETD typically creates very clean MS/MS spectra with intact PTMs. On the HCTultra, the new ETD implementation often provides complete amino acid series down to immonium ion masses, without the low-mass cut-off traditionally encountered in ion trap MS/MS. The combination with the superior mass accuracy of the HCTultra enables powerful de novo sequencing capabilities. Using the PhosphoScan(TM) mode of the HCTultra with ETD offers a unique and powerful system for single run auto-LC/MS/MS/MS CID/ETD experiments specifically for phosphorylation analysis.

Dr. Michael Schubert, Vice President of R&D, stated: "The market-leading acquisition speed and sensitivity of the HCTultra combined with the new information-rich ETD MS/MS capability redefine the ion trap standard for the detection and localization of post-translational modifications, as well as for de novo sequencing of peptides. Its high ion capacity and dynamic range make this system also especially suitable for quantitative proteomics."

ETD and CID data are supported by Bruker Daltonics' bioinformatics suite ProteinScape(TM), which was selected by the HUPO Brain Proteome project as an official tool. It can conveniently handle large numbers of high-quality MS/MS spectra created by the HCTultra in proteomics studies. The HCTultra seamlessly integrates into the Proteineer solution for LC/MS/MS and 2D gel-MS/MS based proteomics projects, as well as into the Metabolic Profiler solution for metabolic studies.

The ETD technique on the HCTultra will be presented in scientific contributions and at the Bruker Daltonics suite at next week's 53rd ASMS conference in San Antonio, Texas.

ABOUT BRUKER BIOSCIENCES (NASDAQ: BRKR)

Bruker BioSciences Corporation, headquartered in Billerica, Massachusetts, is the publicly traded parent company of Bruker AXS Inc. and Bruker Daltonics Inc. Bruker AXS is a leading developer and provider of life science and advanced materials research tools based on X-ray technology. Bruker Daltonics is a leading developer and provider of innovative life science tools based on mass spectrometry. Bruker Daltonics also offers a broad line of nuclear, biological and chemical (NBC) detection products for defense and homeland security. For more information, please visit www.bruker-biosciences.com

CAUTIONARY STATEMENT

Any statements contained in this press release that do not describe historical facts may constitute forward-looking statements as that term is defined in the Private Securities Litigation Reform Act of 1995. Any forward-looking statements contained herein are based on current expectations, but are subject to a number of risks and uncertainties. The factors that could cause actual future results to differ materially from current expectations include, but are not limited to, risks and uncertainties relating to the Company's reorganization strategies, integration risks, failure of conditions, technological approaches, product development, market acceptance, cost and pricing of the Company's products, changes in governmental regulations, capital spending and government funding policies, FDA and other regulatory approvals to the extent applicable, competition, the intellectual property of others, patent protection and litigation. These and other factors are identified and described in more detail in our filings with the SEC, including, without limitation, our annual report on Form 10-K for the year ended December 31, 2004, our most recent quarterly reports on Form 10-Q and our current reports on Form 8-K. We disclaim any intent or obligation to update these forward-looking statements.