2GPN
100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-05-19 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 127.180, 127.180, 115.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.400 - 1.990 |
| R-factor | 0.197 * |
| Rwork | 0.197 |
| R-free | 0.24800 |
| Structure solution method | DIFFERENCE FOURIER |
| Starting model (for MR) | AN UNPUBLISHED 1.5 ANGSTROMS MODEL (E.P.MITCHELL) AND PDB ENTRY 1GPB |
| RMSD bond length | 0.008 * |
| RMSD bond angle | 1.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.400 | 2.140 |
| High resolution limit [Å] | 1.990 | 1.990 |
| Rmerge | 0.114 | 0.373 |
| Total number of observations | 192914 * | |
| Number of reflections | 57703 | |
| <I/σ(I)> | 10.1 | 2.1 |
| Completeness [%] | 89.7 | 89.5 |
| Redundancy | 3.5 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 6.7 | 16 * | THE PROTEIN WAS CRYSTALLIZED FROM 0.01 M BES, PH 6.7, 0.003 M DTT, 0.001 M SPERMINE, 0.0001 M EDTA, 0.02 % (W/V) SODIUM AZIDE AT 16 DEGREES C. THE CRYSTALS WERE CRYOPROTECTED WITH 25% (V/V) MPD (2-METHYL-2,4-PENTANEDIOL)., temperature 289K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 27-28 (mg/ml) | |
| 2 | 1 | 1 | spermine | 1 (mM) | |
| 3 | 1 | 1 | BES | 10 (mM) | |
| 4 | 1 | 1 | dithiothreitol | 3 (mM) | |
| 5 | 1 | 1 | EDTA | 0.1 (mM) | |
| 6 | 1 | 1 | sodium azide | 0.02 (%) |
