1DK0
CRYSTAL STRUCTURE OF THE HEMOPHORE HASA FROM SERRATIA MARCESCENS CRYSTAL FORM P2(1), PH8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-02-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.540, 66.210, 58.930 |
| Unit cell angles | 90.00, 104.91, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.770 |
| R-factor | 0.175 |
| Rwork | 0.169 |
| R-free | 0.21300 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.400 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.820 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.063 | 0.371 |
| Number of reflections | 31089 | |
| <I/σ(I)> | 8.3 | |
| Completeness [%] | 94.4 | 89.3 |
| Redundancy | 5 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 * | 20 * | Arnoux, P., (1999) Nat.Struct.Biol., 6, 516. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | saturated in heme |
| 2 | 1 | reservoir | cacodylate | 100 (mM) | |
| 3 | 1 | reservoir | zinc acetate dihydrate | 140 (mM) | |
| 4 | 1 | reservoir | glycerol | 2 (%) | |
| 5 | 1 | reservoir | PEG8000 | 9-11 (%) |
