Three-dimensional structure of human serum albumin
DC Carter, XM He, SH Munson, PD Twigg, KM Gernert… - Science, 1989 - science.org
DC Carter, XM He, SH Munson, PD Twigg, KM Gernert, MB Broom, TY Miller
Science, 1989•science.orgThe three-dimensional structure of human serum albumin has been solved at 6.0 angstrom
(Å) resolution by the method of multiple isomorphous replacement. Crystals were grown
from solutions of polyethylene glycol in the infrequently observed space group P 4212 (unit
cell constants a= b= 186.5±0.5 Å and c= 81.0±0.5 Å) and diffracted x-rays to lattice d-
spacings of less than 2.9 A. The electron density maps are of high quality and revealed the
structure as a predominantly α-helical globin protein in which the course of the polypeptide …
(Å) resolution by the method of multiple isomorphous replacement. Crystals were grown
from solutions of polyethylene glycol in the infrequently observed space group P 4212 (unit
cell constants a= b= 186.5±0.5 Å and c= 81.0±0.5 Å) and diffracted x-rays to lattice d-
spacings of less than 2.9 A. The electron density maps are of high quality and revealed the
structure as a predominantly α-helical globin protein in which the course of the polypeptide …
The three-dimensional structure of human serum albumin has been solved at 6.0 angstrom (Å) resolution by the method of multiple isomorphous replacement. Crystals were grown from solutions of polyethylene glycol in the infrequently observed space group P4212 (unit cell constants a = b = 186.5 ± 0.5 Å and c = 81.0 ± 0.5 Å) and diffracted x-rays to lattice d-spacings of less than 2.9 A. The electron density maps are of high quality and revealed the structure as a predominantly α-helical globin protein in which the course of the polypeptide can be traced. The binding loci of several organic compounds have been determined.
AAAS