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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 Communications 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.
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
volume
64
issue
Pt 6
pages
516 - 519
publisher
Wiley-Blackwell
external identifiers
  • wos:000256295000016
  • pmid:18540064
  • scopus:46249106074
  • pmid:18540064
ISSN
2053-230X
DOI
10.1107/S1744309108012141
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)
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
2016-04-04 09:27:28
date last changed
2022-01-29 18:00:08
@article{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    = {{Wiley-Blackwell}},
  series       = {{Acta Crystallographica. Section F: Structural Biology and Crystallization Communications}},
  title        = {{Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin.}},
  url          = {{http://dx.doi.org/10.1107/S1744309108012141}},
  doi          = {{10.1107/S1744309108012141}},
  volume       = {{64}},
  year         = {{2008}},
}