2H29
Crystal structure of Nicotinic acid mononucleotide Adenylyltransferase from Staphylococcus aureus: product bound form 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Collection date | 2004-12-01 |
| Wavelength(s) | 1.542 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 118.217, 81.972, 61.942 |
| Unit cell angles | 90.00, 116.39, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.20391 |
| Rwork | 0.202 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.406 |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.200 | |
| Number of reflections | 31473 | |
| <I/σ(I)> | 4.6 | |
| Completeness [%] | 87.9 | 44.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 10mg/ml protein, 50mM Hepes pH 7.2, 300mM KCl, 0.5mM TCEP, 1mM EDTA mixed with equal volume of 10%(w/v) PEG3000, 100mM phosphate-citrate buffer pH4.2, 0.2M NaCl |
