Preliminary Crystallographic Studies of Four Crystal forms of Serum Albumin

Abstract

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 forms produced from human and canine albumin include incorporated long‐chain fatty acids. Molecular replacement experiments have been successfully conducted on each crystal form using the previously determined atomic coordinates of human serum albumin illustrating the conserved tertiary structure. Copyright © 1994, Wiley Blackwell. All rights reserved