1FDW
HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 MUTANT H221Q COMPLEXED WITH ESTRADIOL
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 300 |
Detector technology | AREA DETECTOR |
Collection date | 1994-04 |
Detector | SIEMENS-NICOLET X100 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 123.670, 45.490, 61.630 |
Unit cell angles | 90.00, 98.21, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.700 |
R-factor | 0.178 * |
Rwork | 0.178 |
R-free | 0.26300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fdt |
RMSD bond length | 0.012 |
RMSD bond angle | 0.031 |
Data reduction software | XENGEN |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.800 | 2.830 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.071 * | |
Number of reflections | 6352 | |
Completeness [%] | 65.2 | |
Redundancy | 2.54 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 * | PROTEIN WAS CRYSTALLIZED FROM PEG 4000 30%, 100 MM HEPES BUFFER PH 7.0, 100 MM MGCL2, 0.5 MM ESTRADIOL, PROPANE DIOL 2-4% |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | enzyme | 5 (mg/ml) | |
10 | 1 | 2 | ammonium sulfate | 2-2.4 (M) | |
2 | 1 | 1 | EDTA | 1 (mM) | |
3 | 1 | 1 | dithiothreitol | 0.2 (mM) | |
4 | 1 | 1 | glycerol | 20 (%) | |
5 | 1 | 1 | beta-octylglucoside | 2 (mM) | |
6 | 1 | 2 | sodium phosphate | 100 (mM) | |
7 | 1 | 2 | NAD(P)+ | 1 (mM) | |
8 | 1 | 2 | 100 (mM) | ||
9 | 1 | 2 | decyl-beta-D-maltoside | 2.2-4.4 (mM) | or 9-18mM octyl-beta-D-thioglucopyranoside |