Crystallization of α1-acid glycoprotein

Crystallization and preliminary X-ray analysis of the vitamin D-binding protein from human serum

“…The value of 2.9 A3/dalton is somewhat high and implies a solvent content of about 60%, suggesting the protein to be quite hydrated in the crystal. The value does not, however, appear to be inconsistent with those found for some other glycoproteins [6], and this probably reflects the influence of the ~ar~hydrate moiety. The crystals reported here can be obtained reproducibly and are mechanically sturdy.…”

Crystal growth of cholesterol in hydrogels and its characterization

“…This is due to certain cholesterol conformational states, which need to be detected by the different biological receptors involved in its precipitation [32,33]. In addition, the crystallization of cholesterol in vivo needs a gel-like structure called mucin, which is a glycoprotein commonly observed in bile.…”

Macromolecular Biosensors Based on Proteins Involved in Bile Stones Formation

“…Particularly, orosomucoid a protein of 42 kDa, is one of the most abundant proteins of serum proteins with no well-known physiological function. However, a number of biological activities have been described for orosomucoid, such as promotion of collagen fibril formation, inhibition of platelet aggregation, inhibition of heparin accelerated antithrombin III mediated activation of thrombin and factor Xa, binding of Δ-4 Ketosteroids, sequestration of a glycosaminoglycan cofactor in the lipoprotein lipase reaction and the preferential binding of more than 60 cationic therapeutic drugs [18]. The orosomucoid protein has an unusual pI of around 3 and an extraordinary carbohydrate content of approximately 40% (w/w), comprising five N-linked glycans [19].…”

“…However, although the importance of this orosomucoid in human physiology seems to be high, there are no more structural data from the native glycoprotein obtained at high resolution. The orosomucoid was firstly crystallized in 1984 [18], and since then no more structural data of that native glycoprotein at high resolution have been published. The high-resolution crystallographic structure was not available for a long time.…”

“…This recombinant human AAG produced as monomeric, yet unglycosylated protein in E. coli was obtained via secretion into the bacterial periplasm, where formation of its two-disulphide bonds was facilitated in the oxidizing environment [20]. The former crystals of the native AAG protein were obtained in a hexagonal P622 or P6 2 22 or the enantiomorph P6 4 22 space group in the presence of chlorpromazine at 18 °C [18]. Interestedly, the co-crystallization of the tetragonal AAG by soaking method in the presence of the well-known ligands (phenothiazine tranquilizers) like chlorpromazine, bromazepam or diazepam, failed [20].…”