Welcome to NRAMM
The National Resource for Automated Molecular Microscopy is a Biomedical Technology Research Centers supported by the NIH National Center for Research Resources.
One of the major goals for the current five year grant period is to expand our automated infrastructure in order to provide a complete and integrated pipeline for the reconstruction of macromolecular machines. This infrastructure is primarily aimed at supporting the overall NRAMM mission of developing cryoEM as a mainstream and efficient methodology on a par with, and complementary to, X-ray crystallography. An additional major goal of the core technological and research developments is to address some of the fundamental questions and issues that remain as barriers to deriving high resolution 3D maps of molecular machines using cryoEM. The technology that we are developing provides us with a unique opportunity to systematically probe some of the current limitations of the method.
Recent Featured Image:
Chaperonins GroEL and GroES collaborate in protein folding. A set of cryo-EM structures of GroEL bound to ATP and computational modeling were used to trace the trajectory of sites that bind the substrate, an unfolded or misfolded polypeptide, from their initial positions lining the chaperonin ring through to formation of the folding chamber, which encapsulates but does not bind the substrate. The findings suggest ATP-powered domain twists that may enable the stretching and unfolding of the substrate prior to its release into the folding chamber. From: Clare DK, Vasishtan D, Stagg S, Quispe J, Farr GW, Topf M, et al. ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin. Cell. 2012;149(1):113-23. Epub 2012/03/27. doi: 10.1016/j.cell.2012.02.047. PubMed PMID: 22445172.
See Featured Images pages for more. |
AMI Forums:“Ultrathin silicon-based membranes for separation, concentration, and imaging of biological and nanomaterials” Christopher C. Striemer, Ph.D., Vice President, Membrane Development, SiMPore Inc., West Henrietta, NY Monday, April 30, 2012 @ 12:00 p.m. CIMBio 1st Floor Conference Room Commercially available dialysis and ultrafiltration membranes are commonplace in biotech research, but for many applications, these materials have unacceptably low transport efficiency and are difficult to integrate into micro/nano fabricated systems. We have developed a new class of membrane [Striemer et al., Nature 445, 749, 2007.] that overcomes these limitations with 1) nanoscale thickness, and 2) fabrication on silicon wafer substrates. Nanoscale thickness virtually eliminates the loss of filtrate associated with standard >10 micron thick polymeric membranes and greatly reduces frictional losses, leading to unprecedented transport rates. Their extreme thinness also enables their use in high resolution electron and optical microscopy. Because these membranes are fabricated on planar silicon wafers, system integration is greatly simplified, and scaleable manufacture can be reasonably achieved. We fabricate porous and non-porous membranes that are typically 5 nm – 50 nm thick and free-standing over rectangular apertures measuring up to several millimeters across, depending on the application. The porous nanocrystalline silicon (pnc-Si) membranes are formed by thermal crystallization of thin amorphous silicon films. |
Recent publications acknowledging NRAMM:Baudoux AC, Hendrix RW, Lander GC, Bailly X, Podell S, et al. (2012) Genomic and functional analysis of Vibrio phage SIO-2 reveals novel insights into ecology and evolution of marine siphoviruses. Environ Microbiol. Brilot AF, Chen JZ, Cheng A, Pan J, Harrison SC, et al. (2012) Beam-induced motion of vitrified specimen on holey carbon film. J Struct Biol 177: 630-637. Gibbons BJ, Brignole EJ, Azubel M, Murakami K, Voss NR, et al. (2012) Subunit architecture of general transcription factor TFIIH. Proc Natl Acad Sci U S A 109: 1949-1954. Lander GC, Baudoux AC, Azam F, Potter CS, Carragher B, et al. (2012) Capsomer Dynamics and Stabilization in the T = 12 Marine Bacteriophage SIO-2 and Its Procapsid Studied by CryoEM. Structure 20: 498-503. Lander GC, Estrin E, Matyskiela ME, Bashore C, Nogales E, et al. (2012) Complete subunit architecture of the proteasome regulatory particle. Nature 482: 186-191. Lau P-W, Guiley K, Nabanita D, Potter CS, Carragher B, et al. (2012) The Molecular Architecture of Human Dicer. Nature Structural Molecular Biology Accepted. Moeller A, Zhao C, Fried MG, Wilson-Kubalek EM, Carragher B, et al. (2012) Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly. J Struct Biol 177: 335-343. Scheres SH (2012) A Bayesian View on Cryo-EM Structure Determination. J Mol Biol 415: 406-418. Xu Y, Moeller A, Jun SY, Lee M, Yoon BY, et al. (2012) Assembly and channel opening of the outer membrane protein in tripartite drug efflux pumps of Gram-negative bacteria. J Biol Chem. See publications for a complete list… |
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