Crystallization and preliminary X-ray analysis of fluorescent protein mBanana.
mBanana is a novel monomeric red fluorescent protein mutant. It was cloned and expressed in Escherichia coli with 10 histidine residues at its N-terminal. After cleavage of the His tag by TEV protease, the mBanana was further purified and crystallized by the hanging-drop vapor-diffusion technique. The crystals can diffract to 2.0A resolution and one set of completed data was collected. It showed that the orthorhombic mBanana crystal was in space group P21 with unit cell parameters (48.629, 42.667, 61.714, 90, 111.676, 90) and contained one molecule in one asymmetric unit.
Zhou
Yangbin
Y
Department of Physiology and Biophysics, Fudan University, 200433 Shanghai PR China.
Wu
Yifeng
Y
Song
Jiaping
J
Ding
Yu
Y
Hu
Xiaojian
X
Zhang
Zhihong
Z
D000818:Animals; D037421:Anthozoa / Q000737:chemistry; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008164:Luminescent Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry
D008164:Luminescent Proteins; D011994:Recombinant Proteins