MRI: Acquisition of X-Ray protein crystallography equipment at Northeastern University

MRI:购置东北大学X射线蛋白质晶体学设备

基本信息

  • 批准号:
    1228897
  • 负责人:
  • 金额:
    $ 38.87万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
    Standard Grant
  • 财政年份:
    2012
  • 资助国家:
    美国
  • 起止时间:
    2012-08-01 至 2013-07-31
  • 项目状态:
    已结题

项目摘要

This grant is for the purchase of X-ray macromolecular crystallography equipment at Northeastern University. X-ray crystallography provides one of the most powerful venues for the visualization of proteins and other macromolecules in three dimensions at near atomic resolution. It is at the heart of structural biology, giving access to experimental data that allows scientists to make the connection between what molecules "look like" and how they function. The HighFlux HomeLab, consisting of the Rigaku MicroMax-007HF X-ray generator, with state-of-the-art optics, X-ray detector and cryo-system, enables high-quality crystallographic data collection with secure and automated features that facilitate access to research groups with diverse scientific interests and expertise. Until recently the kind of data that reveals molecular details of biological molecules at atomic resolution, particularly for small and fragile crystals, required travel to national laboratories such as the Advanced Photon Source at Argonne National Laboratory and other synchrotron X-ray sources. Synchrotron facilities are available to a specialized group of scientists with extensive experience in crystallography. The HighFlux HomeLab at Northeastern University will provide the venue for expert X-ray crystallographers to perform cutting edge research with close involvement of graduate and undergraduate students as well as for non-experts to expand the scope of their research to include structural biology. This equipment is highly complementary to structural biology equipment already present at Northeastern in the areas of Nuclear Magnetic Resonance spectroscopy, Mass Spectrometry, Electron Paramagnetic Resonance spectroscopy and computational equipment, thus completing the major set of biophysical approaches used in state of the art structural biology research. Scientific questions being addressed through this project will help elucidate fundamental understanding of cell signaling, DNA damage and repair, enzyme catalysis as well as more practical applications of structural biology to energy production, human disease and biomolecular engineering, the success of which is built on understanding fundamental processes. Central to the use of the X-ray equipment will be a course in Macromolecular Crystallography, staged in the form of a workshop designed to integrate research, teaching and training in structural biology. Northeastern is at the forefront of experiential learning, with a Co-op system that places undergraduates in laboratories across campus, in the Boston area and beyond, for extended periods of full time research. The workshop will have input and support from the PI and coPIs, a facility's manager with a Ph.D. and extensive experience in macromolecular crystallography, an academic specialist and a graduate teaching assistant. This workshop course will welcome faculty, graduate and undergraduate students interested in X-ray data collection, structure refinement and analysis. Students will be encouraged to bring their own crystals, but projects will also be available associated with the PI's and coPI's research groups. As research in the 21st century becomes ever more multidisciplinary, this course will provide "hands on" experience so that researchers in various areas of expertise can integrate structural biology in thinking about their science, with the ability to make a critical assessment not only of structures collected at Northeastern, but also of those deposited in the Protein Data Bank, along with the associated data. The highly integrated research, teaching and learning environment enabled by this project will take place in a very diverse environment in terms of the researchers involved. In addition to being highly productive scholars the senior personnel on this project are diverse in terms of race, ethnicity and gender. Four out of the five are women, one Latina, one Native American and one African American. Current graduate and undergraduate students in the PI's and coPI's laboratories include 26 women, 18 men, 5 African Americans, 2 Native Americans and 1 Latina. Young women and minorities on this project will see the possibilities of success for themselves as reflected in their role models and will be encouraged to continue to do science, helping to increase representation for these groups in our scientific research communities nation wide.
这笔赠款用于购买东北大学的X射线大分子结晶学设备。X射线结晶学为以接近原子分辨率的三维可视化蛋白质和其他大分子提供了最强大的场所之一。它是结构生物学的核心,为科学家提供了获取实验数据的途径,使他们能够在分子的“样子”和它们的功能之间建立联系。HighFlux HomeLab由Rigaku MicroMax-007HF X射线发生器组成,配备最先进的光学系统、X射线探测器和冷冻系统,可实现高质量的晶体数据收集,并具有安全和自动化的功能,便于访问具有不同科学兴趣和专业知识的研究小组。直到最近,这种以原子分辨率揭示生物分子分子细节的数据,特别是小而脆弱的晶体,需要前往国家实验室,如阿贡国家实验室的高级光子源和其他同步辐射X射线源。同步加速器设备可供在结晶学方面拥有丰富经验的科学家组成的专门团队使用。东北大学的HighFlux HomeLab将为专业X射线结晶学家提供场所,在研究生和本科生的密切参与下进行尖端研究,以及为非专家提供场所,以扩大他们的研究范围,包括结构生物学。该设备在核磁共振波谱、质谱学、电子顺磁共振波谱和计算设备领域与东北公司现有的结构生物学设备具有很强的互补性,从而完成了在最先进的结构生物学研究中使用的主要生物物理方法。通过该项目解决的科学问题将有助于阐明对细胞信号、DNA损伤和修复、酶催化以及结构生物学在能源生产、人类疾病和生物分子工程中的更实际应用的基本理解,结构生物学的成功建立在理解基本过程的基础上。使用X射线设备的中心将是一门大分子结晶学课程,该课程将以研讨会的形式举办,旨在整合结构生物学的研究、教学和培训。东北大学在体验式学习方面走在了前列,它的Co-op系统将本科生安排在校园内、波士顿地区以及其他地方的实验室里,进行更长时间的全职研究。研讨会将得到PI和COPIS的投入和支持,他们是一名拥有博士学位并在高分子结晶学方面拥有丰富经验的设施经理,一名学术专家和一名研究生助教。这个工作坊课程将欢迎对X射线数据收集、结构改进和分析感兴趣的教职员工、研究生和本科生。学生们将被鼓励携带他们自己的水晶,但也将提供与PI和COPI的研究小组相关的项目。随着21世纪的研究变得更加多学科,本课程将提供实践经验,使不同专业领域的研究人员能够将结构生物学融入到他们的科学思考中,不仅能够对东北大学收集的结构进行批判性评估,而且还能够对蛋白质数据库中存储的结构以及相关数据进行关键评估。该项目带来的高度一体化的研究、教学和学习环境将在一个非常多样化的环境中进行,涉及的研究人员也不同。除了是高生产率的学者外,该项目的高级人员在种族、族裔和性别方面也是多样化的。五人中有四人是女性,一名拉丁裔,一名原住民和一名非洲裔美国人。目前PI和COPI实验室的研究生和本科生包括26名女性、18名男性、5名非裔美国人、2名美洲原住民和1名拉丁裔。参与这个项目的年轻女性和少数族裔将看到她们的榜样所反映的成功的可能性,并将被鼓励继续从事科学工作,帮助增加这些群体在全国科学研究界的代表性。

项目成果

期刊论文数量(0)
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Carla Mattos其他文献

Locating and characterizing binding sites on proteins
定位和表征蛋白质上的结合位点
  • DOI:
    10.1038/nbt0596-595
  • 发表时间:
    1996-05-01
  • 期刊:
  • 影响因子:
    41.700
  • 作者:
    Carla Mattos;Dagmar Ringe
  • 通讯作者:
    Dagmar Ringe
Analysis of two-residue turns in proteins.
蛋白质中两个残基转角的分析。
  • DOI:
  • 发表时间:
    1994
  • 期刊:
  • 影响因子:
    5.6
  • 作者:
    Carla Mattos;G. Petsko;M. Karplus
  • 通讯作者:
    M. Karplus
Mass spectrometry methods and mathematical PK/PD model for decision tree-guided covalent drug development
用于决策树指导的共价药物开发的质谱方法和数学药代动力学/药效学模型
  • DOI:
    10.1038/s41467-025-56985-6
  • 发表时间:
    2025-02-19
  • 期刊:
  • 影响因子:
    15.700
  • 作者:
    Md Amin Hossain;Rutali R. Brahme;Brandon C. Miller;Jakal Amin;Marcela de Barros;Jaime L. Schneider;Jared R. Auclair;Carla Mattos;Qingping Wang;Nathalie Y. R. Agar;David J. Greenblatt;Roman Manetsch;Jeffrey N. Agar
  • 通讯作者:
    Jeffrey N. Agar

Carla Mattos的其他文献

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{{ truncateString('Carla Mattos', 18)}}的其他基金

Allosteric effects in the complexes between Ras proteins and Raf
Ras 蛋白和 Raf 复合物的变构效应
  • 批准号:
    2121426
  • 财政年份:
    2021
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Standard Grant
Allosteric elements in the superfamily of small GTPases
小 GTP 酶超家族中的变构元素
  • 批准号:
    1517295
  • 财政年份:
    2015
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Standard Grant
REU Site: Research Opportunities in Biological and Chemical Catalysis
REU 网站:生物和化学催化领域的研究机会
  • 批准号:
    1262734
  • 财政年份:
    2013
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Standard Grant
Mechanism of Intrinsic Hydrolysis in Small GTPases
小 GTP 酶的固有水解机制
  • 批准号:
    1244203
  • 财政年份:
    2013
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Continuing Grant
Mining Multiple Solvent Crystal Structures for Properties of Protein Binding Sites
挖掘多种溶剂晶体结构以了解蛋白质结合位点的特性
  • 批准号:
    1237512
  • 财政年份:
    2012
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Continuing Grant
Mining Multiple Solvent Crystal Structures for Properties of Protein Binding Sites
挖掘多种溶剂晶体结构以了解蛋白质结合位点的特性
  • 批准号:
    0818678
  • 财政年份:
    2008
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Continuing Grant
PECASE: Probing protein surfaces using multiple solvent crystal structures
PECASE:使用多种溶剂晶体结构探测蛋白质表面
  • 批准号:
    0237297
  • 财政年份:
    2003
  • 资助金额:
    $ 38.87万
  • 项目类别:
    Continuing Grant

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