Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin.
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1168990
- author
- Pramhed, Anna LU ; Addis, Laura ; Tillgren, Viveka LU ; Wenglén, Christina LU ; Heinegård, Dick LU and Logan, Derek T
- organization
- publishing date
- 2008
- 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}}, }