Development and Evaluation of a Reverse-Entry Ion Source Orbitrap Mass Spectrometer.

Development and Evaluation of a Reverse-Entry Ion Source Orbitrap Mass Spectrometer.
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DOI:
10.1007/s13361-018-1976-0
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发表时间:
2019-01
影响因子:
3.2
通讯作者:
Russell DH
Russell DH
中科院分区:
化学3区
文献类型:
--
作者:
Poltash ML;McCabe JW;Patrick JW;Laganowsky A;Russell DH

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作为利用Orbitrap质谱仪平台开发高分辨率离子迁移率质谱计的一步,我们在这里描述了一种新型的反向进入离子源(REIS),它耦合到具有更大质量范围的Orbitrap质谱仪的高能C陷阱解离(HCD)池。REIS的开发是漂移管离子迁移率-Orbitrap MS开发的第一步。REIS方法保留了商业仪器离子源的功能,允许在开发过程中不间断地使用仪器,以及在两个离子源之间进行性能比较。分别以泛素(8.5 kDa)和脂结合氨转运通道(AmtB,126 kDa)蛋白复合体作为模型可溶性蛋白和膜蛋白,评价该仪器的性能。用REIS获得的质量分辨率与商用离子源获得的质量分辨率相当。在Reis上得到的泛素和AmtB的电荷态分布与前人的研究结果一致,这表明Reis-Orbitrap EMR在气相中保持了自然结构。
As a step towards development of a high-resolution ion mobility mass spectrometer using the orbitrap mass analyzer platform, we describe herein a novel reverse-entry ion source (REIS) coupled to the higher-energy C-trap dissociation (HCD) cell of an orbitrap mass spectrometer with extended mass range. Development of the REIS is a first step in the development of a drift tube ion mobility-orbitrap MS. The REIS approach retains the functionality of the commercial instrument ion source which permits the uninterrupted use of the instrument during development as well as performance comparisons between the two ion sources. Ubiquitin (8.5 kDa) and lipid binding to the ammonia transport channel (AmtB, 126 kDa) protein complex were used as model soluble and membrane proteins, respectively, to evaluate the performance of the REIS instrument. Mass resolution obtained with the REIS is comparable to that obtained using the commercial ion source. The charge state distributions for ubiquitin and AmtB obtained on the REIS are in agreement with previous studies which suggests the REIS - Orbitrap EMR retains native structure in the gas phase.
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