@article {Jun An:2011:0929-8665:858,
title = "Crystallization and Preliminary X-Ray Crystallographic Analysis of CTXM- 15, an Extended-spectrum -Lactamase Conferring Worldwide Emerging Antibiotic Resistance",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2011",
volume = "18",
number = "9",
publication date ="2011-09-01T00:00:00",
pages = "858-862",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2011/00000018/00000009/art00001",
doi = "doi:10.2174/092986611796011400",
keyword = "Polymerase chain reaction, variants, CTX-M-15, polyacrylamide SDS gel, antibiotics, crystal, Antibiotic resistance, liquid nitrogen, nosocomial infections, synchrotron radiation, Cephalosporins, Polyethylene glycol, ceftazidime, lactam ring, third-generation β-lactams, oxyimino β-lactams, ESBLs, Asp240Gly mutation, cefotaxime, extended-spectrum β-lactamase, Escherichia coli",
author = "Jun An, Young and Hun Lee, Jung and Il Jung, Ha and Ghyu Sohn, Seung and Jin Lee, Jae and Seung Park, Kwang and Wu, Xing and Chul Jeong, Byeong and Kang, Choong-Min and Cha, Sun-Shin and Hee Lee, Sang",
abstract = "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 \AA 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 \AA. Analysis of the packing density shows that the asymmetric unit probably contains two molecules with a solvent content of 41.26%. 
",
}