Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli.
Human platelet profilin was expressed in Escherichia coli using a T7 based expression vector. The recombinant material is similar to authentic human platelet profilin based on the measured Kd for rabbit skeletal muscle actin. Crystals of the recombinant material were obtained from both PEG 8000 and (NH4)2SO4. These crystals are isomorphous and belong to the monoclinic space group C2, a = 75.0, b = 32.0, c = 62.5, beta = 123 degrees. These crystals contain one molecule in the asymmetric unit and diffract to at least 2.0 A.
Fedorov
A A
AA
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461.
Pollard
T D
TD
Almo
S C
SC
D000199:Actins / Q000378:metabolism; D001792:Blood Platelets / Q000737:chemistry; D003285:Contractile Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D007700:Kinetics; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D015394:Molecular Structure; D051304:Profilins; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D000199:Actins; D003285:Contractile Proteins; D008840:Microfilament Proteins; C495738:PFN1 protein, human; D051304:Profilins; D011994:Recombinant Proteins