1ZLX
The apo structure of human glycinamide ribonucleotide transformylase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 300 |
Detector technology | IMAGE PLATE |
Collection date | 1996-08-16 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 75.660, 75.660, 101.690 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.200 - 2.200 |
Rwork | 0.224 |
R-free | 0.26700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Truncated (70% remaining) E. coli Glycinamide ribonucleotide transformylase 1GAR |
RMSD bond length | 0.007 |
RMSD bond angle | 1.340 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.200 | 2.150 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 16557 | |
<I/σ(I)> | 8.3 | |
Completeness [%] | 75.8 | 3 |
Redundancy | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 300 | 5 mg/ml protein in 10 mM Hepes pH 7.5, 1 mM DTE 1:1 with well solution (100 mM Na citrate pH 6.0, 20% 2-propanol (v/v), 20% PEG-4000 (w/v)), VAPOR DIFFUSION, HANGING DROP, temperature 300K |
2 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 300 | 5 mg/ml protein in 10 mM Hepes pH 7.5, 1 mM DTE 1:1 with well solution (100 mM Na citrate pH 6.0, 10% 2-propanol (v/v), 18% PEG-4000 (w/v)), pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 300K |