3S0R

Crystal Structure of De novo Designed helical assembly protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.247 
  • R-Value Observed: 0.253 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Computational design of virus-like protein assemblies on carbon nanotube surfaces.

Grigoryan, G.Kim, Y.H.Acharya, R.Axelrod, K.Jain, R.M.Willis, L.Drndic, M.Kikkawa, J.M.DeGrado, W.F.

(2011) Science 332: 1071-1076

  • DOI: https://doi.org/10.1126/science.1198841
  • Primary Citation of Related Structures:  
    3S0R

  • PubMed Abstract: 

    There is a general need for the engineering of protein-like molecules that organize into geometrically specific superstructures on molecular surfaces, directing further functionalization to create richly textured, multilayered assemblies. Here we describe a computational approach whereby the surface properties and symmetry of a targeted surface define the sequence and superstructure of surface-organizing peptides. Computational design proceeds in a series of steps that encode both surface recognition and favorable intersubunit packing interactions. This procedure is exemplified in the design of peptides that assemble into a tubular structure surrounding single-walled carbon nanotubes (SWNTs). The geometrically defined, virus-like coating created by these peptides converts the smooth surfaces of SWNTs into highly textured assemblies with long-scale order, capable of directing the assembly of gold nanoparticles into helical arrays along the SWNT axis.


  • Organizational Affiliation

    Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
De novo designed Helical Assembly
A, B
30synthetic constructMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.247 
  • R-Value Observed: 0.253 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.529α = 90
b = 45.529β = 90
c = 93.293γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
PHASERphasing
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-06-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2011-08-17
    Changes: Source and taxonomy
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references
  • Version 1.4: 2024-04-03
    Changes: Refinement description