Crystallization and preliminary X-ray investigation of a ubiquitin carrier protein (E2) from Arabidopsis thaliana.
Crystals of a recombinant ubiquitin carrier protein from Arabidopsis thaliana have been grown from solutions of ammonium sulfate. The crystals are orthorhombic, space group P2(1)2(1)2(1); the axes are a = 41.8(1) A, b = 44.9(1) A and c = 83.2(1) A. The crystals are quite stable to X-rays and diffract beyond 2.1 A resolution. There is one molecule in the asymmetric unit.
Cook
W J
WJ
Department of Pathology, University of Alabama, Birmingham 35294.
Jeffrey
L C
LC
Sullivan
M L
ML
Vierstra
R D
RD
D002352:Carrier Proteins / Q000648:ultrastructure*; D003461:Crystallography; D008025:Ligases; D010940:Plant Proteins / Q000648:ultrastructure*; D010944:Plants; D011994:Recombinant Proteins / Q000648:ultrastructure; D044763:Ubiquitin-Conjugating Enzymes; D014452:Ubiquitins / Q000378:metabolism*; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D010940:Plant Proteins; D011994:Recombinant Proteins; D014452:Ubiquitins; C046288:ubiquitin carrier proteins; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases