@article {5414,
	title = {Purification, characterization, and crystallization of human pyrroline-5-carboxylate reductase.},
	journal = {Protein Expression and Purification},
	volume = {49},
	year = {2006},
	month = {2006 Sep},
	pages = {83-7},
	abstract = {<p>Pyrroline-5-carboxylate reductase (P5CR) catalyzes the reduction of Delta1-pyrroline-5-carboxylate (P5C) to proline with concomitant oxidation of NAD(P)H to NAD(P)(+). The enzymatic cycle between P5C and proline is very important in many physiological and pathological processes. Human P5CR was over-expressed in Escherichia coli and purified to homogeneity by chromatography. Enzymatic assays of the wild-type protein were carried out using 3,4-dehydro-L-proline as substrate and NAD(+) as cofactor. The homopolymer was characterized by cross-linking and size exclusion gel filtration chromatography. Human P5CR was crystallized by the hanging-drop vapor-diffusion method at 37 degrees C. Diffraction data were obtained to a resolution of 2.8A and were suitable for high resolution X-ray structure determination.</p>
},
	keywords = {Crystallization, Crystallography, Gene Expression, Humans, Polymers, Proline, Pyrroline Carboxylate Reductases, Solubility, Water, X-Ray},
	issn = {1046-5928},
	doi = {10.1016/j.pep.2006.02.019},
	author = {Meng, Zhaohui and Lou, Zhiyong and Liu, Zhe and Hui, Dong and Bartlam, Mark and Rao, Zihe}
}
