1MB1
MBP1 FROM SACCHAROMYCES CEREVISIAE
Experimental procedure
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE AREA DETECTOR |
Collection date | 1997-01 |
Detector | MARRESEARCH |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 42.580, 42.580, 123.680 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 2.100 |
R-factor | 0.215 * |
Rwork | 0.215 |
R-free | 0.29000 |
Structure solution method | MAD |
RMSD bond length | 0.016 |
RMSD bond angle | 2.470 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CCP4 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 2.160 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.041 | 0.124 |
Number of reflections | 6810 | |
<I/σ(I)> | 30 | 11 |
Completeness [%] | 94.4 | 93.3 |
Redundancy | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.9 | 4 * | Taylor, I.A., (1997) Proteins Struct. Funct. Genet., 27,325. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG3350 | 28-30 (%(w/v)) | |
2 | 1 | reservoir | Tris-HCl | 50 (mM) | |
3 | 1 | reservoir | 200 (mM) |