Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory
Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electro...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Satoh, Takaya [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2007 |
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| Schlagwörter: |
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| Anmerkung: |
© American Society for Mass Spectrometry 2007 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of the American Society for Mass Spectrometry - Springer-Verlag, 1990, 18(2007), 7 vom: 01. Juli, Seite 1318-1323 |
|---|---|
| Übergeordnetes Werk: |
volume:18 ; year:2007 ; number:7 ; day:01 ; month:07 ; pages:1318-1323 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.jasms.2007.04.010 |
|---|
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OLC2097673716 |
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| 520 | |a Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. | ||
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10.1016/j.jasms.2007.04.010 doi (DE-627)OLC2097673716 (DE-He213)j.jasms.2007.04.010-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Satoh, Takaya verfasserin aut Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory 2007 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2007 Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. Mass Accuracy Calibration Equation Sinapic Acid MALDI Target Grid Electrode Sato, Takafumi aut Tamura, Jun aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 18(2007), 7 vom: 01. Juli, Seite 1318-1323 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:18 year:2007 number:7 day:01 month:07 pages:1318-1323 https://doi.org/10.1016/j.jasms.2007.04.010 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 GBV_ILN_4313 AR 18 2007 7 01 07 1318-1323 |
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10.1016/j.jasms.2007.04.010 doi (DE-627)OLC2097673716 (DE-He213)j.jasms.2007.04.010-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Satoh, Takaya verfasserin aut Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory 2007 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2007 Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. Mass Accuracy Calibration Equation Sinapic Acid MALDI Target Grid Electrode Sato, Takafumi aut Tamura, Jun aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 18(2007), 7 vom: 01. Juli, Seite 1318-1323 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:18 year:2007 number:7 day:01 month:07 pages:1318-1323 https://doi.org/10.1016/j.jasms.2007.04.010 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 GBV_ILN_4313 AR 18 2007 7 01 07 1318-1323 |
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10.1016/j.jasms.2007.04.010 doi (DE-627)OLC2097673716 (DE-He213)j.jasms.2007.04.010-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Satoh, Takaya verfasserin aut Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory 2007 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2007 Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. Mass Accuracy Calibration Equation Sinapic Acid MALDI Target Grid Electrode Sato, Takafumi aut Tamura, Jun aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 18(2007), 7 vom: 01. Juli, Seite 1318-1323 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:18 year:2007 number:7 day:01 month:07 pages:1318-1323 https://doi.org/10.1016/j.jasms.2007.04.010 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 GBV_ILN_4313 AR 18 2007 7 01 07 1318-1323 |
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10.1016/j.jasms.2007.04.010 doi (DE-627)OLC2097673716 (DE-He213)j.jasms.2007.04.010-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Satoh, Takaya verfasserin aut Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory 2007 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2007 Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. Mass Accuracy Calibration Equation Sinapic Acid MALDI Target Grid Electrode Sato, Takafumi aut Tamura, Jun aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 18(2007), 7 vom: 01. Juli, Seite 1318-1323 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:18 year:2007 number:7 day:01 month:07 pages:1318-1323 https://doi.org/10.1016/j.jasms.2007.04.010 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 GBV_ILN_4313 AR 18 2007 7 01 07 1318-1323 |
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| title_auth |
Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory |
| abstract |
Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. © American Society for Mass Spectrometry 2007 |
| abstractGer |
Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. © American Society for Mass Spectrometry 2007 |
| abstract_unstemmed |
Abstract A novel MALDI-TOF mass spectrometer that utilizes a spiral ion trajectory was developed. In this mass spectrometer, the ions sequentially passed through four toroidal electrostatic sectors and revolved along a figure-eight-shaped orbit on a particular projection plane. Each toroidal electrostatic sector had eight stories, and during multiple revolutions, the ion trajectory shifted perpendicular to the projection plane in every cycle, thereby generating a spiral trajectory. The flight path length of one cycle was 2.1 m; therefore, when the ions completed eight cycles, the total flight path length was 17 m. By adopting an ion optical system that had a flight path length five times longer than that in the commonly used reflectron ion optical system, the mass dependence on the mass resolving power was reduced, while improving the mass accuracy of the mass measurements. The basic performance of the system was tested by using standard peptides or the tryptic digest of bovine serum albumin. A mass resolving power of 80,000 (full width at half maximum) was achieved at m/z=2564 (ACTH18-39). An improved mass accuracy less than 2 ppm was realized over a wide m/z range of 500 to 3000 by correction using one or two internal standard substances. © American Society for Mass Spectrometry 2007 |
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| container_issue |
7 |
| title_short |
Development of a high-Performance MALDI-TOF mass spectrometer utilizing a spiral ion trajectory |
| url |
https://doi.org/10.1016/j.jasms.2007.04.010 |
| remote_bool |
false |
| author2 |
Sato, Takafumi Tamura, Jun |
| author2Str |
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| doi_str |
10.1016/j.jasms.2007.04.010 |
| up_date |
2024-07-03T14:14:03.359Z |
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