Expression, crystallization and preliminary crystallographic analysis of the extracellular IgV-like domain of the human natural killer cell inhibitory receptor p75/AIRM1

Nazzareno Dimasi, Lorenzo Moretta, Roberto Biassoni, Roy A. Mariuzza

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

p75/AIRM1 (Siglec-7) is a sialic acid-binding Ig-like lectin recently identified as an inhibitory receptor on natural killer cells. The expression, in vitro folding, circular-dichroism spectroscopy, crystallization and preliminary X-ray characterization of the Ig-V like domain of p75/AIRM1 are reported. X-ray data were collected from a single crystal at 100 K, with a maximum useful diffraction pattern extending to 1.45 Å resolution on a synchrotron source. The crystal belongs to a primitive monoclinic space group, with unit-cell parameters a = 32.65, b = 49.72, c = 39.79 Å, α = γ = 90, β = 113°. The systematic absences indicate that the space group is P21. Assuming one molecule per asymmetric unit, V M (the Matthews coefficient) was calculated to be 1.879 Å 3Da-1 and the solvent content was estimated to be 32.01%.

Original languageEnglish
Pages (from-to)1856-1858
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume59
Issue number10
DOIs
Publication statusPublished - Oct 1 2003

Fingerprint

Sialic Acid Binding Immunoglobulin-like Lectins
Natural Killer Cell Receptors
Crystallization
X-Rays
crystallization
Circular dichroism spectroscopy
X rays
Synchrotrons
Circular Dichroism
cells
folding
Diffraction patterns
dichroism
Spectrum Analysis
synchrotrons
x rays
diffraction patterns
Single crystals
Crystals
acids

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

@article{4a02fbe0aed64fa4989709cf9fdac007,
title = "Expression, crystallization and preliminary crystallographic analysis of the extracellular IgV-like domain of the human natural killer cell inhibitory receptor p75/AIRM1",
abstract = "p75/AIRM1 (Siglec-7) is a sialic acid-binding Ig-like lectin recently identified as an inhibitory receptor on natural killer cells. The expression, in vitro folding, circular-dichroism spectroscopy, crystallization and preliminary X-ray characterization of the Ig-V like domain of p75/AIRM1 are reported. X-ray data were collected from a single crystal at 100 K, with a maximum useful diffraction pattern extending to 1.45 {\AA} resolution on a synchrotron source. The crystal belongs to a primitive monoclinic space group, with unit-cell parameters a = 32.65, b = 49.72, c = 39.79 {\AA}, α = γ = 90, β = 113°. The systematic absences indicate that the space group is P21. Assuming one molecule per asymmetric unit, V M (the Matthews coefficient) was calculated to be 1.879 {\AA} 3Da-1 and the solvent content was estimated to be 32.01{\%}.",
author = "Nazzareno Dimasi and Lorenzo Moretta and Roberto Biassoni and Mariuzza, {Roy A.}",
year = "2003",
month = "10",
day = "1",
doi = "10.1107/S0907444903018146",
language = "English",
volume = "59",
pages = "1856--1858",
journal = "Acta Crystallographica Section D: Biological Crystallography",
issn = "0907-4449",
publisher = "International Union of Crystallography",
number = "10",

}

TY - JOUR

T1 - Expression, crystallization and preliminary crystallographic analysis of the extracellular IgV-like domain of the human natural killer cell inhibitory receptor p75/AIRM1

AU - Dimasi, Nazzareno

AU - Moretta, Lorenzo

AU - Biassoni, Roberto

AU - Mariuzza, Roy A.

PY - 2003/10/1

Y1 - 2003/10/1

N2 - p75/AIRM1 (Siglec-7) is a sialic acid-binding Ig-like lectin recently identified as an inhibitory receptor on natural killer cells. The expression, in vitro folding, circular-dichroism spectroscopy, crystallization and preliminary X-ray characterization of the Ig-V like domain of p75/AIRM1 are reported. X-ray data were collected from a single crystal at 100 K, with a maximum useful diffraction pattern extending to 1.45 Å resolution on a synchrotron source. The crystal belongs to a primitive monoclinic space group, with unit-cell parameters a = 32.65, b = 49.72, c = 39.79 Å, α = γ = 90, β = 113°. The systematic absences indicate that the space group is P21. Assuming one molecule per asymmetric unit, V M (the Matthews coefficient) was calculated to be 1.879 Å 3Da-1 and the solvent content was estimated to be 32.01%.

AB - p75/AIRM1 (Siglec-7) is a sialic acid-binding Ig-like lectin recently identified as an inhibitory receptor on natural killer cells. The expression, in vitro folding, circular-dichroism spectroscopy, crystallization and preliminary X-ray characterization of the Ig-V like domain of p75/AIRM1 are reported. X-ray data were collected from a single crystal at 100 K, with a maximum useful diffraction pattern extending to 1.45 Å resolution on a synchrotron source. The crystal belongs to a primitive monoclinic space group, with unit-cell parameters a = 32.65, b = 49.72, c = 39.79 Å, α = γ = 90, β = 113°. The systematic absences indicate that the space group is P21. Assuming one molecule per asymmetric unit, V M (the Matthews coefficient) was calculated to be 1.879 Å 3Da-1 and the solvent content was estimated to be 32.01%.

UR - http://www.scopus.com/inward/record.url?scp=0141959890&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0141959890&partnerID=8YFLogxK

U2 - 10.1107/S0907444903018146

DO - 10.1107/S0907444903018146

M3 - Article

VL - 59

SP - 1856

EP - 1858

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

SN - 0907-4449

IS - 10

ER -