Crystallization of an intact GST-estrogen receptor hormone binding domain fusion protein.
Crystals of an intact GST-estrogen receptor hormone binding domain fusion protein have been grown from solutions of MPD. The crystals grew as clusters of thin plates and needles of maximum dimensions 100 x 20 x 1 micrometer but were unsuitable for X-ray diffraction analysis. However, examination by electron microscopy shows an ordered lattice in which the protein molecules are clearly visible. Image analysis of electron micrographs of the protein crystals revealed electron stain-excluding density which showed a two-domain trimeric structure in projection, with each molecule of dimensions 12.0 x 5.0 nm diameter. The use of GST-fusion proteins in crystallisation are discussed.
Lally
J M
JM
Protein Structure Laboratory, Imperial Cancer Research Fund, 44 Lincolns Inn Fields, London WC2A 3PX, England.
Newman
R H
RH
Knowles
P P
PP
Islam
S
S
Coffer
A I
AI
Parker
M
M
Freemont
P S
PS
D003460:Crystallization; D005982:Glutathione Transferase / Q000737:chemistry*; D008024:Ligands; D008854:Microscopy, Electron; D017434:Protein Structure, Tertiary; D011960:Receptors, Estrogen / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
D008024:Ligands; D011960:Receptors, Estrogen; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase