Purification, crystallization and preliminary X-ray investigation of the complex of human vitamin D binding protein and rabbit muscle actin.
The vitamin D binding protein binds globular actin with high affinity and is involved in the clearance of actin from the blood circulation. A complex of the human vitamin D binding protein and rabbit muscle actin was subjected to purification steps. The pure complex was crystallized using the hanging-drop vapour-diffusion procedure. The best obtained crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 74.44, b = 74.90, c = 88.02 A, beta = 110.19 degrees. A complete data set to 2.4 A was collected from a single crystal using synchrotron radiation at DESY, Hamburg, Germany.
Bogaerts
I
I
Laboratorium voor Analytische Chemie en Medicinale Fysicochemie, Faculteit Farmaceutische Wetenschappen, K. U. Leuven, E. Van Evenstraat 4, 3000 Leuven, Belgium.
Verboven
C
C
Rabijns
A
A
Waelkens
E
E
Van Baelen
H
H
De Ranter
C
C
D000199:Actins / Q000737:chemistry* / Q000302:isolation & purification; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009132:Muscles / Q000737:chemistry*; D011487:Protein Conformation; D011817:Rabbits; D014809:Vitamin D-Binding Protein / Q000737:chemistry* / Q000302:isolation & purification
D000199:Actins; D014809:Vitamin D-Binding Protein