Difference: JoachimFrank (1 vs. 13)
Revision 1321 Jan 2010 - Main.DavidCowburn
| ||||||||
| Changed: | ||||||||
| < < |
| |||||||
| > > |
| |||||||
| ||||||||
| Added: | ||||||||
| > > | Email address is for AA | |||||||
|
Publicly available grant information
Grant Number: 7R01GM029169-27 Project Title: STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLY PI Information: Name Email Title FRANK, JOACHIM jf2192@columbia.edu PROFESSOR Abstract: DESCRIPTION (provided by applicant): Cryo-EM combined with single-particle reconstruction, a method pioneered in the Pi's lab, is capable of visualizing macromolecular machines such as transcription complexes, chaperones, or ribosomes under native conditions in different functional states. The goal of attaining 10 A for the ribosome, a structure without symmetry, has driven development of data collection and image processing techniques in our lab. This goal has been achieved, thanks to consistent funding of this grant from NIH. The dissemination of software (SPIDER) has benefited the research of other groups on numerous other biological structures. In the study of translation, density maps for a broad range of functional complexes in the resolution range of 9-13 A, interpreted by fitting of X-ray structures, have greatly advanced our knowledge of factor binding and our understanding of the dynamics of translation. A new resolution goal is set in Specific Aim #1 of the present proposal: the achievement of atomic (~3A) resolution for certain ribosomal complexes known to be highly stable. This goal requires simultaneous efforts in several areas: (i) exploration of grid preparation parameters that lead to uniform layers of ice with optimum thickness; (ii) large increase in data collected (~10-fold, for a yield of 1,000,000 "good particles"), requiring an increased level of automation and computational resources; (iii) strategies for carrying out CTF correction; (iv) angular refinement methods, which must be accelerated and improved through design and implementation of more efficient algorithms and computational strategies; (v) methods for fitting and docking of X-ray structures into density maps must be explored. Specific Aim #2 concerns the elucidation, at near-atomic resolution, of a pivotal step (GTP hydrolysis) in mRNA-tRNA translocation both in eubacteria and eukaryotes, to be achieved by application of the technology developed and implemented in Specific Aim #1 to specific complexes with proven stability. Already along the way toward the goal of 3 A, we can expect that new discoveries will be made due to the improved definition of rRNA structure, as well as protein subdomains and structural motifs such as a-helices and -?-sheets, allowing conformational changes and molecular interactions during translocation to be modeled and described with much higher precision. To achieve these goals, we collaborate with key experts in the areas of reconstruction algorithms, ribosome biochemistry, X-ray crystallography, and computational modeling. Public Health Relevance: This Public Health Relevance is not available. Thesaurus Terms: There are no thesaurus terms on file for this project. Institution: COLUMBIA UNIVERSITY HEALTH SCIENCES Columbia University Medical Center NEW YORK, NY 100323702 Fiscal Year: 2008 Department: BIOCHEM & MOLECULAR BIOPHYSICS Project Start: 01-APR-1982 Project End: 31-MAR-2011 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: BBM Grant Number: 7R01GM055440-12 Project Title: EXPERIMENTALLY GUIDED RIBOSOMAL RNA MODELING PI Information: Name Email Title FRANK, JOACHIM jf2192@columbia.edu PROFESSOR Abstract: This abstract is not available. Public Health Relevance: This Public Health Relevance is not available. Thesaurus Terms: There are no thesaurus terms on file for this project. Institution: COLUMBIA UNIVERSITY HEALTH SCIENCES Columbia University Medical Center NEW YORK, NY 100323702 Fiscal Year: 2008 Department: BIOCHEM & MOLECULAR BIOPHYSICS Project Start: 01-JAN-1997 Project End: 31-MAR-2010 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: ZRG1 | ||||||||
Revision 1225 Sep 2008 - Main.DavidCowburn
| ||||||||
| Added: | ||||||||
| > > | ||||||||
| Grant Number: 7R01GM029169-27 Project Title: STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLY PI Information: Name Email Title FRANK, JOACHIM jf2192@columbia.edu PROFESSOR Abstract: DESCRIPTION (provided by applicant): Cryo-EM combined with single-particle reconstruction, a method pioneered in the Pi's lab, is capable of visualizing macromolecular machines such as transcription complexes, chaperones, or ribosomes under native conditions in different functional states. The goal of attaining 10 A for the ribosome, a structure without symmetry, has driven development of data collection and image processing techniques in our lab. This goal has been achieved, thanks to consistent funding of this grant from NIH. The dissemination of software (SPIDER) has benefited the research of other groups on numerous other biological structures. In the study of translation, density maps for a broad range of functional complexes in the resolution range of 9-13 A, interpreted by fitting of X-ray structures, have greatly advanced our knowledge of factor binding and our understanding of the dynamics of translation. A new resolution goal is set in Specific Aim #1 of the present proposal: the achievement of atomic (~3A) resolution for certain ribosomal complexes known to be highly stable. This goal requires simultaneous efforts in several areas: (i) exploration of grid preparation parameters that lead to uniform layers of ice with optimum thickness; (ii) large increase in data collected (~10-fold, for a yield of 1,000,000 "good particles"), requiring an increased level of automation and computational resources; (iii) strategies for carrying out CTF correction; (iv) angular refinement methods, which must be accelerated and improved through design and implementation of more efficient algorithms and computational strategies; (v) methods for fitting and docking of X-ray structures into density maps must be explored. Specific Aim #2 concerns the elucidation, at near-atomic resolution, of a pivotal step (GTP hydrolysis) in mRNA-tRNA translocation both in eubacteria and eukaryotes, to be achieved by application of the technology developed and implemented in Specific Aim #1 to specific complexes with proven stability. Already along the way toward the goal of 3 A, we can expect that new discoveries will be made due to the improved definition of rRNA structure, as well as protein subdomains and structural motifs such as a-helices and -?-sheets, allowing conformational changes and molecular interactions during translocation to be modeled and described with much higher precision. To achieve these goals, we collaborate with key experts in the areas of reconstruction algorithms, ribosome biochemistry, X-ray crystallography, and computational modeling. Public Health Relevance: This Public Health Relevance is not available. Thesaurus Terms: There are no thesaurus terms on file for this project. Institution: COLUMBIA UNIVERSITY HEALTH SCIENCES Columbia University Medical Center NEW YORK, NY 100323702 Fiscal Year: 2008 Department: BIOCHEM & MOLECULAR BIOPHYSICS Project Start: 01-APR-1982 Project End: 31-MAR-2011 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: BBM | ||||||||
| Added: | ||||||||
| > > | Grant Number: 7R01GM055440-12 Project Title: EXPERIMENTALLY GUIDED RIBOSOMAL RNA MODELING PI Information: Name Email Title FRANK, JOACHIM jf2192@columbia.edu PROFESSOR Abstract: This abstract is not available. Public Health Relevance: This Public Health Relevance is not available. Thesaurus Terms: There are no thesaurus terms on file for this project. Institution: COLUMBIA UNIVERSITY HEALTH SCIENCES Columbia University Medical Center NEW YORK, NY 100323702 Fiscal Year: 2008 Department: BIOCHEM & MOLECULAR BIOPHYSICS Project Start: 01-JAN-1997 Project End: 31-MAR-2010 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: ZRG1 | |||||||
Revision 1125 Sep 2008 - Main.DavidCowburn
| ||||||||
| Added: | ||||||||
| > > | Publicly available grant information Grant Number: 7R01GM029169-27 Project Title: STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLY PI Information: Name Email Title FRANK, JOACHIM jf2192@columbia.edu PROFESSOR Abstract: DESCRIPTION (provided by applicant): Cryo-EM combined with single-particle reconstruction, a method pioneered in the Pi's lab, is capable of visualizing macromolecular machines such as transcription complexes, chaperones, or ribosomes under native conditions in different functional states. The goal of attaining 10 A for the ribosome, a structure without symmetry, has driven development of data collection and image processing techniques in our lab. This goal has been achieved, thanks to consistent funding of this grant from NIH. The dissemination of software (SPIDER) has benefited the research of other groups on numerous other biological structures. In the study of translation, density maps for a broad range of functional complexes in the resolution range of 9-13 A, interpreted by fitting of X-ray structures, have greatly advanced our knowledge of factor binding and our understanding of the dynamics of translation. A new resolution goal is set in Specific Aim #1 of the present proposal: the achievement of atomic (~3A) resolution for certain ribosomal complexes known to be highly stable. This goal requires simultaneous efforts in several areas: (i) exploration of grid preparation parameters that lead to uniform layers of ice with optimum thickness; (ii) large increase in data collected (~10-fold, for a yield of 1,000,000 "good particles"), requiring an increased level of automation and computational resources; (iii) strategies for carrying out CTF correction; (iv) angular refinement methods, which must be accelerated and improved through design and implementation of more efficient algorithms and computational strategies; (v) methods for fitting and docking of X-ray structures into density maps must be explored. Specific Aim #2 concerns the elucidation, at near-atomic resolution, of a pivotal step (GTP hydrolysis) in mRNA-tRNA translocation both in eubacteria and eukaryotes, to be achieved by application of the technology developed and implemented in Specific Aim #1 to specific complexes with proven stability. Already along the way toward the goal of 3 A, we can expect that new discoveries will be made due to the improved definition of rRNA structure, as well as protein subdomains and structural motifs such as a-helices and -?-sheets, allowing conformational changes and molecular interactions during translocation to be modeled and described with much higher precision. To achieve these goals, we collaborate with key experts in the areas of reconstruction algorithms, ribosome biochemistry, X-ray crystallography, and computational modeling. Public Health Relevance: This Public Health Relevance is not available. Thesaurus Terms: There are no thesaurus terms on file for this project. Institution: COLUMBIA UNIVERSITY HEALTH SCIENCES Columbia University Medical Center NEW YORK, NY 100323702 Fiscal Year: 2008 Department: BIOCHEM & MOLECULAR BIOPHYSICS Project Start: 01-APR-1982 Project End: 31-MAR-2011 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: BBM | |||||||
Revision 1025 Sep 2008 - Main.DavidCowburn
| ||||||||
| Added: | ||||||||
| > > | ||||||||
Revision 925 Sep 2008 - Main.DavidCowburn
| ||||||||
| Added: | ||||||||
| > > | ||||||||
Personal Preferences (details in TWikiVariables)
| ||||||||
Revision 809 Aug 2008 - Main.DavidCowburn
| ||||||||
| Changed: | ||||||||
| < < |
| |||||||
| > > |
| |||||||
| Deleted: | ||||||||
| < < | Biochemistry & Molecular Biophysics; tb2319@columbia.edu; (212) 305-9512; | |||||||
Personal Preferences (details in TWikiVariables)
| ||||||||
Revision 709 Aug 2008 - Main.DavidCowburn
| ||||||||
| Changed: | ||||||||
| < < |
| |||||||
| > > |
| |||||||
| Added: | ||||||||
| > > | Biochemistry & Molecular Biophysics; tb2319@columbia.edu; (212) 305-9512; | |||||||
Personal Preferences (details in TWikiVariables)
| ||||||||
Revision 609 Aug 2008 - Main.DavidCowburn
|
Revision 508 Aug 2008 - Main.DavidCowburn
|
Revision 416 Jul 2008 - Main.DavidCowburn
| ||||||||
| Changed: | ||||||||
| < < |
| |||||||
| > > |
| |||||||
| ||||||||
Revision 316 Jul 2008 - Main.DavidCowburn
|
Revision 216 Jun 2008 - Main.JasperShahn
| ||||||||
| Changed: | ||||||||
| < < |
| |||||||
| > > |
| |||||||
| Deleted: | ||||||||
| < < |
| |||||||
Revision 115 Aug 2005 - Main.JoachimFrank
|
View topic
| History: r13 < r12 < r11 < r10
| More topic actions...
Copyright © by the contributing authors. All material on this collaboration platform is the property of the contributing authors.
Ideas, requests, problems regarding this intranet, Send feedback
Ideas, requests, problems regarding this intranet, Send feedback