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1J9M

K38H mutant of Streptomyces K15 DD-transpeptidase

Replaces:  1EQS
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-3
Synchrotron siteESRF
BeamlineID14-3
Temperature [K]100
Detector technologyCCD
Collection date1999-06-05
DetectorMARRESEARCH
Wavelength(s)0.933
Spacegroup nameP 21 21 21
Unit cell lengths45.596, 53.638, 104.690
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 1.650
R-factor0.218
Rwork0.218
R-free0.25600
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007
RMSD bond angle1.200
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]34.7101.600
High resolution limit [Å]1.5601.560
Rmerge0.0380.139
Number of reflections343321069

*

<I/σ(I)>19.13
Completeness [%]91.7

*

39.7
Redundancy3.71.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.220

*

Tris 0.1 M, PEG 6K 30%, NaCl 0.4 M, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein2.3-20 (mg/ml)
21reservoirTris-HCl0.1 (M)
31reservoir0.5 (M)
41reservoirPEG6000

227111

PDB entries from 2024-11-06

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