Crystal structure of isozyme 4-4 and molecular modeling of isozyme 3-4 of class mu glutathione S-transferases from rat liver
Year: 1996
Type: article
Abstract: MACROMOLECULES C-111three-dimensional intensity data were collected by imaging plate diffractometer of RIGAKU RAXIS He.The average figure of merit at 3.0 A resolution is 0.43, using "mlphare" in~ CCP4 program package.The phase improvement was can•ied out by ''dm" in CCP4, resulting in a 2.2 A resolution density map.The density modification includes histogram-mapping, constraint of Sayer formula, non-crystallographic averaging and solvent flattening, with assumption of 41% solvent content.The final free-R-value was 0.27 at 2.2 A resolution.Two identical molecules are in the crystallographic asymmetric unit.The two molecules are related by 143 degree rotation around an axis almost parallel to the crystallographic z axis with some translation.Each molecule consists of two domains.TheN-terminal domain has five helices and seven ~-strands (ex/~ structure) with two additional long helices inN-ten11inus.The C-terminal domain is mainly composed ofleft-handed ~-helix similar to the structure of UDP-N-acetylglucosamineacyltransferasel).The protein structure is under refinement with program X-PLOR. 1) C.
Authors: G. Xiao, X. Ji, R. Armstrong, G. L. Gilliland
Institution: Freie Universität Berlin
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2332329492