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1MQF

Compound I from Proteus mirabilis catalase

Replaces:  2CAF
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyAREA DETECTOR
Collection date1995-10-13
DetectorMARRESEARCH
Wavelength(s)0.98
Spacegroup nameP 62 2 2
Unit cell lengths110.000, 110.000, 250.000
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution15.000

*

- 2.500
R-factor0.196
Rwork0.196
R-free0.23400
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.013
RMSD bond angle24.300

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000

*

2.600
High resolution limit [Å]2.5002.500
Rmerge0.044

*

0.104

*

Total number of observations138931

*

Number of reflections30822

*

<I/σ(I)>10.76.7
Completeness [%]98.3

*

97.1

*

Redundancy4.54.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5

*

4-5

*

Jouve, H.M., (1991) J.Mol.Biol., 221, 1075.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein27 (mg/ml)
21dropTris-HCl100 (mM)
31dropglycerol2.5 (%(v/v))
41dropammonium sulfate1 (M)
51drop25 (mM)
61reservoirammonium sulfate2 (M)
71reservoir50 (mM)
81reservoirTris-HCl100 (mM)

222624

PDB entries from 2024-07-17

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