Crystallization and preliminary crystallographic study of HIP/PAP, a human C-lectin overexpressed in primary liver cancers

Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1487-9. doi: 10.1107/s0907444999007969.

Abstract

Human HIP/PAP is an adhesion protein expressed in normal pancreatic and Paneth cells and overexpressed in hepatocellular carcinoma. HIP/PAP was crystallized using the Hampton Research Crystal Screen and SAmBA software to define the optimal crystallization protocol. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 30.73, b = 49.35, c = 92.15 A and one molecule in the asymmetric unit. Flash-frozen crystals diffract to 1. 78 A resolution using synchrotron radiation. A molecular-replacement solution was obtained using the human Reg/lithostathine structure and the AMoRe software.

MeSH terms

  • Acute-Phase Proteins / chemistry*
  • Acute-Phase Proteins / genetics
  • Acute-Phase Proteins / isolation & purification*
  • Animals
  • Antigens, Neoplasm*
  • Biomarkers, Tumor / chemistry*
  • Biomarkers, Tumor / genetics
  • Biomarkers, Tumor / isolation & purification*
  • Carcinoma, Hepatocellular / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Female
  • Humans
  • Lectins / chemistry*
  • Lectins / genetics
  • Lectins / isolation & purification*
  • Lectins, C-Type*
  • Liver Neoplasms / chemistry*
  • Mice
  • Mice, Transgenic
  • Milk / chemistry
  • Pancreatitis-Associated Proteins
  • Proteins*

Substances

  • Acute-Phase Proteins
  • Antigens, Neoplasm
  • Biomarkers, Tumor
  • Lectins
  • Lectins, C-Type
  • Pancreatitis-Associated Proteins
  • Proteins
  • REG3A protein, human
  • Reg3b protein, mouse