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1LHY

Crystal structure of TEM-30 beta-Lactamase at 2.0 Angstrom

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 5ID-B
Synchrotron siteAPS
Beamline5ID-B
Temperature [K]100
Detector technologyCCD
Collection date2001-12-19
DetectorMARRESEARCH
Wavelength(s)1.0000
Spacegroup nameP 21 21 21
Unit cell lengths41.532, 59.670, 88.097
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution17.000 - 2.000
Rwork0.176
R-free0.21200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)PDB ID 1JWP
RMSD bond length0.009
RMSD bond angle21.700

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]17.0002.070
High resolution limit [Å]2.0002.000
Rmerge0.0880.342
Total number of observations75684

*

Number of reflections14828
<I/σ(I)>16.63.6
Completeness [%]96.498.4
Redundancy5.15
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8295used seeding

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
21dropsodium potassium Pi buffer0.65 (M)pH8.0
31reservoirsodium potassium Pi buffer1.4 (M)pH8.0

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