1B67
CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X31 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1995-09-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 33.720, 52.580, 67.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 11.000 - 1.480 |
R-factor | 0.188 |
R-free | 0.26600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | NMR MODEL OF HMFB |
RMSD bond length | 0.010 |
RMSD bond angle | 0.028 |
Data reduction software | DENZO |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | AMoRE ((CCP4)) |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 11.000 | 1.530 |
High resolution limit [Å] | 1.480 | 1.480 |
Rmerge | 0.057 * | 0.256 * |
Total number of observations | 77006 * | |
Number of reflections | 20445 * | |
<I/σ(I)> | 2.9 | 2.9 |
Completeness [%] | 99.1 | 100 |
Redundancy | 3.8 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | CRYSTALLISATION IN HANGING DROP RESERVOIR: 2.6 M (NH4)2SO4 PROTEIN WAS MIXED 1 TO 1 WITH RESERVOIR SOLUTION, pH 6.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-20 (mg/ml) | |
2 | 1 | reservoir | potassium citrate | 100 (mM) | |
3 | 1 | reservoir | Tris-HCl | 50 (mM) |