Preliminary crystallographic study of a complex formed between the alpha/beta-tubulin heterodimer and the neuronal growth-associated protein SCG10

J Struct Biol. 2000 Aug;131(2):156-8. doi: 10.1006/jsbi.2000.4283.

Abstract

Crystals of a complex formed between the alpha/beta-tubulin heterodimer and SCG10, a neuron-specific growth-associated protein, have been obtained by the hanging drop method. They belong to the space group P2(1)2(1)2(1), with unit cell parameters a = 56 A, b = 353 A, c = 466 A and four molecular complexes in the asymmetric unit. A complete X-ray diffraction data set to 6.1 A resolution has been collected using synchrotron radiation. This represents a challenging opportunity to study at a molecular level the structure-function relationships between a microtubule-destabilizing protein, SCG10, and tubulin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain / metabolism
  • Cattle
  • Crystallization
  • Dimerization
  • Macromolecular Substances
  • Nerve Growth Factors / chemistry*
  • Nerve Growth Factors / metabolism*
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Protein Binding
  • Protein Structure, Quaternary
  • Tubulin / chemistry*
  • Tubulin / metabolism*
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Nerve Growth Factors
  • Nerve Tissue Proteins
  • Tubulin