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2CC1

Crystal structure of the class A beta-lactamase from Mycobacterium fortuitum

Replaces:  1MFO
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsLURE BEAMLINE DW32
Synchrotron siteLURE
BeamlineDW32
Temperature [K]300
Spacegroup nameP 21 21 21
Unit cell lengths35.660, 73.420, 91.320
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution57.260 - 2.130
R-factor0.169
Rwork0.167
R-free0.22400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1bsg
RMSD bond length0.020
RMSD bond angle1.923
Phasing softwareAMoRE
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]57.2602.180
High resolution limit [Å]2.1302.130
Rmerge0.060
Number of reflections11576
Completeness [%]86.953
Redundancy2.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1

220113

PDB entries from 2024-05-22

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