Hostname: page-component-848d4c4894-pjpqr Total loading time: 0 Render date: 2024-06-22T20:37:04.743Z Has data issue: false hasContentIssue false

Exploring Macromolecular Interactions at High Resolution Using Electron Cryomicroscopy at NCMI

Published online by Cambridge University Press:  02 July 2020

M.F. Schmid
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
M. B. Sherman
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
J. Brink
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
J. Jakana
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
M. Kelsey
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
M. Dougherty
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
W. Chiu
Affiliation:
Verna and Marrs McLean Department of Biochemistry, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX77030
Get access

Extract

The National Center for Macromolecular Imaging (NCMI) is a resource supported by the National Center for Research Resources (NCRR) of NIH. Its mission is to advance electron imaging of macromolecular assemblies to near atomic resolution. We have focused on biological assemblies which are too large or too complex to be studied by conventional x-ray crystallography or NMR spectroscopy techniques. As is the case with all the NCRR-supported facilities, we also conduct methodology development, collaboration, service, technology dissemination and training.

The objectives of this Research Resource are to develop the technology of high resolution electron cryomicroscopy of biological macromolecules, assemblies and crystals in an integrated approach that includes specimen preparation, hardware and software development. A current methodology development includes the characterization of the 1k x 1k slow-scan CCD camera for both electron diffraction and imaging of ice-embedded specimens. These studies have defined the advantages and limitations of the CCD camera for electron crystallographic analysis. Another core research project deals with the problems of specimen movement due to the electron beam and/or charging and seeks to minimize these phenomena. Our efforts have resulted in a better understanding of the physics of charging. We have modified a Gatan ion-beam coater so that we can apply a thin layer of carbon onto ice-embedded specimens.

Type
Shared Resources: Access to Critical Instrumentation
Copyright
Copyright © Microscopy Society of America 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Brink, J.et al., J. Struct. Biol. 113(1994)23.10.1006/jsbi.1994.1029CrossRefGoogle Scholar
2.Sherman, M.B.et al., Micron 27(1996)129.10.1016/0968-4328(96)00018-2CrossRefGoogle Scholar
3.Brink, J.et al., Ultramicroscopy 46(1992)229.10.1016/0304-3991(92)90017-ECrossRefGoogle Scholar
4.Brink, J.et al., in Proc. XI EUREM (Dublin, 1996).Google Scholar
5.Hardt, S.et al., J. Struct. Biol. 116(1996)68.10.1006/jsbi.1996.0012CrossRefGoogle Scholar
6.Brink, J.et al., J. Struct. Biol. 116(1996)144.10.1006/jsbi.1996.0023CrossRefGoogle Scholar
7.Thuman-Commike, P.A.et al., J. Struct. Biol. 116(1996)41.10.1006/jsbi.1996.0008CrossRefGoogle Scholar
8.Avila-Sakar, A.J., et al, Biophys. J. 70(1996)57.10.1016/S0006-3495(96)79597-8CrossRefGoogle Scholar
9.Schmid, M.F.et al., J. Cell Biol. 124(1994)341.10.1083/jcb.124.3.341CrossRefGoogle Scholar
10.Schmid, M.F.et al., J. Struct. Biol. 115(1995)209.10.1006/jsbi.1995.1045CrossRefGoogle Scholar
11.Zhou, Z.H.et al., Nature Struct. Biol. 2(1995) 1026.10.1038/nsb1195-1026CrossRefGoogle Scholar
12.Thuman-Commike, P.A.et al.,7. Mol. Biol. 260(1996)85.10.1006/jmbi.1996.0383CrossRefGoogle Scholar
13.Orlova, E.V.et al., Nature Struct. Biol. 3(1996)547.10.1038/nsb0696-547CrossRefGoogle Scholar
14.Chiu, W.et al., J. Struct. Biol. 115(1995)117.10.1006/jsbi.1995.1036CrossRefGoogle Scholar
15.Chiu, W.et al., J. Struct. Biol, in press(1997).Google Scholar
16. This work is supported by NIH-RR02250 and NSF BIR-9500098.Google Scholar