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Crystallographic protein model-building on the web.

Kreshna Gopal1, Erik McKee, Tod Romo

  • 1Department of Computer Science, Texas A&M University, 301 H.R. Bright Building, College Station, TX 77843-3112, USA. textal@tamu.edu

Bioinformatics (Oxford, England)
|December 2, 2006
PubMed
Summary
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WebTex automates protein model-building by fitting atoms into electron density maps, accelerating structural biology research. This web interface enhances the TEXTAL program for faster protein structure determination.

Area of Science:

  • Structural biology
  • Biochemistry
  • Computational biology

Background:

  • X-ray crystallography is a primary method for determining protein 3D structures.
  • Model-building, involving fitting atomic structures into electron density maps, is a critical and often time-consuming step.
  • Automated interpretation of electron density maps can significantly improve the efficiency of structure determination.

Purpose of the Study:

  • To introduce WebTex, a web interface for the TEXTAL program.
  • To provide an automated solution for fitting atoms into electron density maps during protein model-building.

Main Methods:

  • Development of WebTex, a user-friendly web interface.
  • Integration of WebTex with the TEXTAL program for automated model-building.

Related Experiment Videos

  • TEXTAL facilitates the process of fitting atomic models into electron density maps.

    • Main Results:

    • WebTex offers a simple yet powerful tool for automating a key step in protein crystallography.
    • The TEXTAL program, accessible via WebTex, automates the fitting of atoms into electron density maps.
    • The system aims to enhance throughput in protein structure determination pipelines.

    Conclusions:

    • Automated model-building tools like WebTex and TEXTAL are crucial for advancing structural biology.
    • WebTex provides an accessible platform for researchers to utilize automated protein model-building.
    • The developed interface and program can accelerate the process of determining protein structures.