TY - JOUR
T1 - Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis
AU - Frias, Janice A.
AU - Goblirsch, Brandon R.
AU - Wackett, Lawrence P.
AU - Wilmot, Carrie M.
PY - 2010/9
Y1 - 2010/9
N2 - OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4 Å resolution. The crystals belonged to space group P3121 or P3221, with unit-cell parameters a = b = 98.8, c = 141.0 Å.
AB - OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4 Å resolution. The crystals belonged to space group P3121 or P3221, with unit-cell parameters a = b = 98.8, c = 141.0 Å.
KW - OleC
KW - hydrocarbon biosynthesis
UR - http://www.scopus.com/inward/record.url?scp=77956554265&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77956554265&partnerID=8YFLogxK
U2 - 10.1107/S1744309110031751
DO - 10.1107/S1744309110031751
M3 - Article
C2 - 20823539
AN - SCOPUS:77956554265
SN - 1744-3091
VL - 66
SP - 1108
EP - 1110
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 9
ER -