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Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin.

Pramhed, Anna LU ; Addis, Laura; Tillgren, Viveka LU ; Wenglén, Christina LU ; Heinegård, Dick LU and Logan, Derek T (2008) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00 64(Pt 6). p.516-519
Abstract
Chondroadherin is a cartilage matrix protein that is known to mediate the adhesion of isolated chondrocytes. Its protein core is composed of 11 leucine-rich repeats flanked by cysteine-rich domains at the N- and C-terminal ends. Recombinant human chondroadherin was crystallized using the sitting-drop vapour-diffusion method. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 56.4, b = 111.3, c = 128.5 A, beta = 92.2, and are most likely to contain four molecules in the asymmetric unit. The crystals diffracted to at least 2.3 A using synchrotron radiation, but structure determination using molecular replacement has so far been unsuccessful.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00
volume
64
issue
Pt 6
pages
516 - 519
publisher
Wiley-Blackwell
external identifiers
  • WOS:000256295000016
  • PMID:18540064
  • Scopus:46249106074
ISSN
2053-230X
DOI
10.1107/S1744309108012141
language
English
LU publication?
yes
id
84bdf0f3-6368-42f8-bc44-360702720595 (old id 1168990)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18540064?dopt=Abstract
date added to LUP
2008-07-03 11:23:07
date last changed
2016-11-10 15:42:44
@misc{84bdf0f3-6368-42f8-bc44-360702720595,
  abstract     = {Chondroadherin is a cartilage matrix protein that is known to mediate the adhesion of isolated chondrocytes. Its protein core is composed of 11 leucine-rich repeats flanked by cysteine-rich domains at the N- and C-terminal ends. Recombinant human chondroadherin was crystallized using the sitting-drop vapour-diffusion method. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 56.4, b = 111.3, c = 128.5 A, beta = 92.2, and are most likely to contain four molecules in the asymmetric unit. The crystals diffracted to at least 2.3 A using synchrotron radiation, but structure determination using molecular replacement has so far been unsuccessful.},
  author       = {Pramhed, Anna and Addis, Laura and Tillgren, Viveka and Wenglén, Christina and Heinegård, Dick and Logan, Derek T},
  issn         = {2053-230X},
  language     = {eng},
  number       = {Pt 6},
  pages        = {516--519},
  publisher    = {ARRAY(0xa9c5d68)},
  series       = {Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00},
  title        = {Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin.},
  url          = {http://dx.doi.org/10.1107/S1744309108012141},
  volume       = {64},
  year         = {2008},
}