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| Item Type: | Article |
|---|---|
| Title: | Purification and preliminary X-ray crystallographic studies of beta-microseminoprotein from human seminal plasma |
| Creators Name: | Kumar, V., Roske, Y., Singh, N., Heinemann, U., Singh, T.P. and Yadav, S. |
| Abstract: | beta-Microseminoprotein (beta-MSP) is a small cysteine-rich protein with a molecular mass of 10 kDa. It was first isolated from human seminal plasma and has subsequently been identified from several species. Comparison of the amino-acid sequences of beta-MSP proteins suggests that the protein is a rapidly evolving protein. The function of beta-MSP is poorly understood. Furthermore, no crystal structure has been reported of any beta-MSP; therefore, determination of the crystal structure of beta-MSP is the foremost task in order to understand the function of this protein completely. Here, the purification, crystallization and preliminary X-ray diffraction analysis of beta-MSP from human seminal plasma are described. The protein was purified using anion-exchange and size-exclusion chromatography and the purified protein was crystallized using 0.1 M ammonium sulfate, 0.1 M HEPES buffer pH 7.0 and 20%(w/v) PEG 3350. The crystals belonged to the tetragonal space group P4(3)22 and contained three beta-MSP molecules in the asymmetric unit. X-ray intensity data were collected to 2.4 A resolution. |
| Keywords: | Crystallization, X-Ray Crystallography, Prostatic Secretory Proteins, Semen |
| Source: | Acta Crystallographica Section F |
| ISSN: | 1744-3091 |
| Publisher: | International Union of Crystallography |
| Volume: | 65 |
| Number: | 5 |
| Page Range: | 518-521 |
| Date: | 1 May 2009 |
| Official Publication: | https://doi.org/10.1107/S1744309109013670 |
| PubMed: | View item in PubMed |
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