1999/06/01 by Shigetoshi Sugio, Akiko Kashima, Shota Mochizuki +2 · 10 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Biochemistry #Chemistry #Crystal (programming language) #Crystal structure #Crystallography #Cysteine #Disulfide Linkage #Enzyme Structure and Function #Human serum albumin #Molecular replacement #Molecule #Multiple isomorphous replacement #Organic chemistry #Peptide sequence #Protein Interaction Studies and Fluorescence Analysis #Protein Structure and Dynamics #Resolution (logic) #Triclinic crystal system
paper · doi:10.1093/protein/12.6.439
openalex publication_date 1999/06/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.