Expression, purification, crystallization and preliminary X-ray characterization of the GRP carbohydrate-recognition domain from Homo sapiens.
Galectins are a family of animal lectins which share similar carbohydrate-recognition domains (CRDs) and an affinity for beta-galactosides. A novel human galectin-related protein named GRP (galectin-related protein; previously known as HSPC159) comprises only one conserved CRD with 38 additional N-terminal residues. The C-terminal fragment of human GRP (GRP-C; residues 38-172) containing the CRD has been expressed and purified. The protein was crystallized using the hanging-drop vapour-diffusion method from a solution containing 2% PEG 400 and 2M ammonium sulfate in 100 mM Tris-HCl buffer pH 7.5. Diffraction data were collected to a resolution limit of 2.0 angstroms at beamline 3W1A of Beijing Synchrotron Radiation Facility at 100 K. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 123.07, b = 96.67, c = 61.56 angstroms, beta = 118.72 degrees. The estimated Matthews coefficient was 2.6 angstroms3 Da(-1), corresponding to 51.8% solvent content.
Zhou
Dongwen
D
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.
Sun
Jianping
J
Zhao
Wei
W
Zhang
Xiao
X
Shi
Yunyu
Y
Teng
Maikun
M
Niu
Liwen
L
Dong
Yuhui
Y
Liu
Peng
P