2BFZ
Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20mM ZnSO4 in buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-03-30 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 67.309, 67.309, 177.604 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.300 |
| R-factor | 0.1819 |
| Rwork | 0.182 |
| R-free | 0.23870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bc2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.370 |
| 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] | 9.900 | 2.360 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.150 | 0.510 |
| Number of reflections | 20328 | |
| <I/σ(I)> | 5.3 | 1.6 |
| Completeness [%] | 95.8 | 95.8 |
| Redundancy | 3.5 | 3.5 |
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 |
