2BG8
Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT and 1mM TCEP-HCl were used as reducing agents.
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 | 2002-05-31 |
| Detector | ADSC CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 67.250, 67.250, 177.800 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.500 |
| R-factor | 0.1849 |
| Rwork | 0.185 |
| R-free | 0.23740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bc2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.330 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 58.000 | 2.570 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.110 | 0.320 |
| Number of reflections | 16423 | |
| <I/σ(I)> | 6 | 2.2 |
| Completeness [%] | 98.5 | 99.5 |
| Redundancy | 4.3 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 291 | PROTEIN WAS CRYSTALLISED USING HANGING DROP VAPOR DIFFUSION. RESERVOIR SOLUTION CONTAINED 100MM TRIS AT PH4.5-5, 70-75% AMMONIUM SULPHATE, 1MM DTT OR 1MM DTT AND 1MM TCEP-HCL, 2MM ZNSO4 AND 0.1% AZIDE. PROTEIN CONCENTRATION OF 2.7 MG/ML. DROPS WERE KEPT AT 291K AND WERE STREAK SEEDED FROM A WILD TYPE CRYSTAL AFTER 1 DAY., PH 4.50 |
