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Welcome

IMP's broad goal is to contribute to a comprehensive structural characterization of biomolecules ranging in size and complexity from small peptides to large macromolecular assemblies. Detailed structural characterization of assemblies is generally impossible by any single existing experimental or computational method. This barrier can be overcome by hybrid approaches that integrate data from diverse biochemical and biophysical experiments (eg, x-ray crystallography, NMR spectroscopy, electron microscopy, immuno-electron microscopy, footprinting, chemical cross-linking, FRET spectroscopy, small angle X-ray scattering, immunoprecipitation, genetic interactions, etc...).

We formulate the hybrid approach to structure determination as an optimization problem, the solution of which requires three main components:

  • the representation of the assembly,
  • the scoring function and
  • the optimization method.

The ensemble of solutions to the optimization problem embodies the most accurate structural characterization given the available information.

We created IMP, the Integrative Modeling Platform, to make it easier to implement such an integrative approach to structural and dynamics problems. IMP is designed to allow mixing and matching of existing modeling components as well as easy addition of new functionality. We encourage and support contributions from other laboratories through the IMP Community.

If you use IMP, please cite D. Russel, K. Lasker, B. Webb, D. Schneidman, J. Velázquez-Muriel, A. Sali, "Putting the pieces together: integrative structure determination of macromolecular assemblies", PLoS Biology, 2012. The main page of each IMP module in the documentation also lists publications relevant to that module.

The IMP software is used as part of the NCDIR logo National Center for Dynamic Interactome Research (NCDIR).

News

IMP 2.0.1 is released! Get it from the download page.

Please imp at salilab.org | email us if you have questions about IMP.

Highlighted research

IMP has been employed to translate tethered conformation capture (TCC) data into physical chromatin contacts in a population of three-dimensional genome structures. Statistical analysis of the resulting population demonstrates that the indiscriminate properties of interchromosomal interactions are consistent with the well-known architectural features of the human genome. more...

IMP has been used by researchers at the Centro de Investigación Príncipe Felipe in Spain, in combination with chromosome conformation capture carbon copy (5C) technology, to generate high-resolution three-dimensional models of chromatin at the megabase scale. [publication 1]   [publication 2]

Researchers from UCSF and the Rockefeller University have used IMP for modeling the Nuclear Pore Complex. more...

Highlighted development

The IMP 2.0.1 release contains several new applications to tackle certain modeling problems, including
  • EMageFit to build assembly models using electron microscopy images (class averages)
  • multifit and cnmultifit to build assembly models using electron microscopy density maps
  • Integrative docking to improve pairwise docking using a variety of additional experimental information sources
  • saxs_merge, a fully automated statistical method for merging small-angle X-ray (SAXS) profiles using Gaussian processes