2H2A
Crystal structure of Nicotinic acid mononucleotide adenylyltransferase from Staphylococcus aureus: product bound form 2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 175 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-12-01 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.303, 83.649, 99.113 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.202 |
| Rwork | 0.200 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h29 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.746 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| 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 | 0.099 | 0.532 |
| Number of reflections | 35401 | |
| <I/σ(I)> | 25.3 | 2.83 |
| Completeness [%] | 99.4 | 94.6 |
| Redundancy | 6.1 | 4.7 |
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 in equal volume of 20% PEG8000(w/v), 100mM MES pH 6.0, 0.2M Ca(OAc)2 |
