Preliminary crystallographic studies of four 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 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.
Carter
D C
DC
Biophysics Branch, Marshall Space Flight Center, Alabama 35812.
Chang
B
B
Ho
J X
JX
Keeling
K
K
Krishnasami
Z
Z
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004285:Dogs; D005227:Fatty Acids / Q000737:chemistry; D010215:Papio; D011994:Recombinant Proteins / Q000737:chemistry; D012709:Serum Albumin / Q000737:chemistry*
D005227:Fatty Acids; D011994:Recombinant Proteins; D012709:Serum Albumin