Crystallization and preliminary X-ray study of the deaminase AmnE from Pseudomonas sp. AP-3. Corrigendum
نویسندگان
چکیده
In the article by Yu et al. (2013) the Matthews coefficient and solvent content are incorrect. The correct Matthews coefficient should be 2.10 Å Da 1 instead of 3.15 Å Da , corresponding to a solvent content of 41.53% instead of 61.02%. In Table 1 the resolution range should be 50.00–2.09 Å. The number of observed reflections should be 319580 (10109) instead of 22932 (752), and the number of unique reflections should be 23327 (1087) instead of 14970 (708).
منابع مشابه
Crystallization and preliminary X-ray study of the deaminase AmnE from Pseudomonas sp. AP-3.
The amnE gene from Pseudomonas sp. AP-3 has been verified as encoding a deaminase with 142 amino-acid residues. In order to change the substrate specificity via structure-based protein engineering, the amnE gene, after gene-code optimization, was chemically synthesized and cloned into the expression vector pET-28a. The protein was expressed in Escherichia coli BL21 (DE3) and purified by Ni(2+)-...
متن کاملCrystallization and preliminary x-ray crystallographic data of dienelactone hydrolase from Pseudomonas sp. B13.
Dienelactone hydrolase (EC 3.1.1.45) from Pseudomonas sp. B13 has been crystallized in a form suitable for high resolution x-ray diffraction study. The crystals are orthorhombic, the space group being P212121, with unit cell dimensions a = 48.9 A, b = 71.2 A, and c = 77.5 A. There appears to be 1 molecule in the asymmetric unit.
متن کاملCrystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses an early step of the tetrapyrrole-biosynthesis pathway in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. The enzyme possesses a dipyrromethane cofactor which is covalently linked by a thioether bridge to an invariant cysteine residue. Expression ...
متن کاملCrystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus. Corrigendum
DNA topoisomerase IV removes undesirable topological features from DNA molecules in order to help maintain chromosome stability. Two constructs of 56 and 59 kDa spanning the DNA-cleavage domain of the A subunit of topoisomerase IV from Staphylococcus aureus (termed GrlA56 and GrlA59) have been crystallized. Crystals were grown at 291 K using the sitting-drop vapour-diffusion technique with PEG ...
متن کاملPurification, crystallization and preliminary X-ray analysis of IMP-18, a class B carbapenemase from Pseudomonas aeruginosa.
Class B β-lactamases are known as metallo-β-lactamases (MBLs) and they hydrolyze most β-lactams, including carbapenems. IMP-18, an MBL cloned from Pseudomonas aeruginosa, was overexpressed, purified and crystallized by vapour diffusion for X-ray crystallographic analysis. Preliminary X-ray analysis showed that the crystal diffracted to 2.4 Å resolution and belonged to the tetragonal space group...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره 69 شماره
صفحات -
تاریخ انتشار 2013