PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF 4 CRYSTAL FORMS OF SERUM-ALBUMIN

Several crystal forms of serum albumin suitable for three-dimensional structure determination have been grown. These forms include crystals of recombinant and wild-type human serum albumin, baboon serum albumin , and canine serum albumin. The intrinsic limits of X-ray diffraction for these crystals are in the range 0.28-0.22 nm. Two of the crystal f orms produced from human and canine albumin include incorporated long- chain fatty acids. Molecular replacement experiments have been success fully conducted on each crystal form using the previously determined a tomic coordinates of human serum albumin illustrating the conserved te rtiary structure.