1AXK
ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 123 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-08 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.270, 133.700, 77.950 |
| Unit cell angles | 90.00, 99.76, 90.00 |
Refinement procedure
| Resolution | 19.960 - 2.100 |
| R-factor | 0.177 |
| Rwork | 0.176 |
| R-free | 0.22400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CIRCULARLY PERMUTED 1 3-1 4-ENDO-BETA-GLUCANASE CPMAC57 (PDB ENTRY 1CPN) AND BACILLUS CIRCULANS 1 3-ENDO-BETA-XYLANASE (PDB ENTRY 1BCX). |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.031 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.058 | 0.230 |
| Total number of observations | 165157 * | |
| Number of reflections | 48499 | |
| <I/σ(I)> | 11.6 | 3.3 |
| Completeness [%] | 91.3 | 80 |
| Redundancy | 3.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.7 * | pH 8.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2.8 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 2 (mM) | ||
| 4 | 1 | reservoir | KP | 40 (mM) | |
| 5 | 1 | reservoir | PEG8000 | 16 (%) |
