Crystallization and preliminary X-ray diffraction studies of a corrinoid protein from Sporomusa ovata.
Crystals of a 40 kDa p-cresolyl-cobamide containing protein from Sporomusa ovata have been obtained from polyethyleneglycol solutions at pH 8.5 by the hanging drop technique. The crystals belong to space group C222(1) with cell dimensions a = 110.5(0.2) A, b = 144.0 (0.2) A, c = 110.4 (0.1) A. They diffract to 2.2 A resolution on a rotating anode X-ray source and are suitable for high resolution X-ray diffraction studies.
Wagner
U G
UG
Institut für Physikalische Chemie, Karl-Franzes-Universität Graz, Austria.
Stupperich
E
E
Aulkemeyer
P
P
Kratky
C
C
D001105:Archaea / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D045728:Corrinoids; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D007202:Indicators and Reagents; D008970:Molecular Weight; D011166:Porphyrins / Q000032:analysis*; D011487:Protein Conformation
D001426:Bacterial Proteins; D045728:Corrinoids; D007202:Indicators and Reagents; D011166:Porphyrins