Open AccessCrystallization and preliminary X‐ray analysis of human liver α‐enolase
Author(s) -
Wang Juan,
Zhou YanFeng,
Li LanFen,
Su XiaoDong
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109004138
Subject(s) - crystallization , enolase , human liver , materials science , crystallography , chemistry , medicine , biochemistry , enzyme , immunohistochemistry , organic chemistry
Enolase is a multifunctional enzyme that plays important roles in many biological and disease processes. α‐Enolase from human liver (hENO1) was expressed as a soluble protein and purified by affinity column chromatography and gel filtration. Crystals were obtained by the hanging‐drop vapour‐diffusion method and diffracted to 2.5 Å resolution. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 72.85, b = 66.02, c = 79.43 Å, β = 94.54°.