1FIZ
THREE DIMENSIONAL STRUCTURE OF BETA-ACROSIN FROM BOAR SPERMATOZOA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX14.1 |
Synchrotron site | SRS |
Beamline | PX14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-02-03 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 43 3 2 |
Unit cell lengths | 130.640, 130.640, 130.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.900 |
Rwork | 0.212 |
R-free | 0.26518 |
RMSD bond length | 0.029 |
RMSD bond angle | 2.650 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 3.100 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.078 | 0.307 |
Number of reflections | 8711 * | |
<I/σ(I)> | 18.6 | |
Completeness [%] | 97.4 | 99.8 |
Redundancy | 5.9 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.2 * | 291 | PEG 8000, ammonium sulphate, sodium cacodylate, p-aminobenzamidine, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 18K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | L-BAPNA | 0.375 (mM) | |
2 | 1 | drop | Tris-HCl | 0.1 (M) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | protein | 20mg | |
5 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
6 | 1 | reservoir | PEG8000 | 30 (%) | |
7 | 1 | reservoir | ammonium sulfate | 0.2 (M) |