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

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.

SUBMITTER: Pramhed A

PROVIDER: S-EPMC2496858 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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

Pramhed Anna A Addis Laura L Tillgren Viveka V Wenglén Christina C Heinegård Dick D Logan Derek T DT

Acta crystallographica. Section F, Structural biology and crystallization communications 20080523 Pt 6

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 molecul ...[more]

PMID: 18540064

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