Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin.
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.
Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, S-221 00 Lund, Sweden.
Anna
A
Pramhed
Laura
L
Addis
Viveka
V
Tillgren
Christina
C
Wenglén
Dick
D
Heinegård
Derek T
DT
Logan
D003460:Crystallization; D016326:Extracellular Matrix Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D006801:Humans; D000090263:Leucine-Rich Repeat Proteins; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods*
D016326:Extracellular Matrix Proteins; D000090263:Leucine-Rich Repeat Proteins; D011506:Proteins; C088980:chondroadherin