4D1C
STRUCTURE OF MHP1, A NUCLEOBASE-CATION-SYMPORT-1 FAMILY TRANSPORTER, IN A CLOSED CONFORMATION WITH bromovinylhydantoin bound.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 287 |
| Detector technology | CCD |
| Collection date | 2010-07-18 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 90.012, 107.323, 109.255 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.896 - 3.700 |
| R-factor | 0.2599 |
| Rwork | 0.257 |
| R-free | 0.28750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4d1a |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.112 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.760 |
| High resolution limit [Å] | 3.700 | 3.700 |
| Rmerge | 0.070 | 0.530 |
| Number of reflections | 11569 | |
| <I/σ(I)> | 15 | 2 |
| Completeness [%] | 98.0 | 98 |
| Redundancy | 4.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | PROTEIN WAS CRYSTALLIZED FROM 27-33 % PEG 300, 0.1M NACL AND 0.1M NA-PHOSPHATE (PH 7.0). BROMOVINYLHYDANTOIN WAS ADDED TO THE DROP AS A SATURATED SOLUTION. |
