| Autor: |
Jun An, Young, Hun Lee, Jung, Il Jung, Ha, Ghyu Sohn, Seung, Jin Lee, Jae, Seung Park, Kwang, Wu, Xing, Chul Jeong, Byeong, Kang, Choong-Min, Cha, Sun-Shin, Hee Lee, Sang |
| Zdroj: |
Protein and Peptide Letters; September 2011, Vol. 18 Issue: 9 p858-862, 5p |
| Abstrakt: |
CTX-M-15, an extended-spectrum -lactamase emerging worldwide, hydrolyzes lactam ring of -lactam antibiotics, and thus causes therapeutic failure and a lack of eradication of pathogenic bacteria by third-generation -lactams. Therefore, the enzyme is a potential target for developing agents against pathogens isolated from patients suffering from nosocomial infections. The CTX-M-15 protein was purified and crystallized at 298 K. X-ray diffraction data from CTXM- 15 crystal have been collected to 1.46 Å resolution using synchrotron radiation. The crystal of CTX-M-15 belongs to space group P212121, with unit-cell parameters a 45.50, b 44.23, and c 116.92 Å. Analysis of the packing density shows that the asymmetric unit probably contains two molecules with a solvent content of 41.26. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
