Crystallization and preliminary crystallographic study of human lithostathine

Proteins. 1995 Dec;23(4):604-6. doi: 10.1002/prot.340230418.

Abstract

Crystals of human lithostathine, a pancreatic glycoprotein which inhibits the growth and nucleation of calcium carbonate crystals, were grown using PEG 4000 as the precipitating agent. The crystals belong to the hexagonal space group P6(1) (or its enantiomorph P6(5)) and diffract to 1.55 A resolution. There is one molecule in the asymmetric unit and the crystals have 39% solvent.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / isolation & purification
  • Carrier Proteins / chemistry
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Lithostathine
  • Mannose / metabolism
  • Mannose-Binding Lectins
  • Molecular Sequence Data
  • Nerve Tissue Proteins*
  • Pancreatic Juice
  • Phosphoproteins / chemistry
  • Protein Conformation*
  • Rats
  • Sequence Homology, Amino Acid
  • Software

Substances

  • Calcium-Binding Proteins
  • Carrier Proteins
  • Lithostathine
  • Mannose-Binding Lectins
  • Nerve Tissue Proteins
  • Phosphoproteins
  • REG1A protein, human
  • Reg1a protein, rat
  • Mannose