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1K9O

CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX

Replaces:  1I99
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date1999-12-10
Wavelength(s)1.03320
Spacegroup nameP 31 2 1
Unit cell lengths112.572, 112.572, 95.955
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 2.300
R-factor0.158

*

Rwork0.158
R-free0.23100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)PDB ENTRIES 1SEK AND 1DPO
RMSD bond length0.008
RMSD bond angle1.610
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.380
High resolution limit [Å]2.3002.300
Rmerge0.0910.391
Total number of observations186342

*

Number of reflections30999
<I/σ(I)>11.31.76
Completeness [%]98.495.6
Redundancy66
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.5298PEG 3350, DTT, POTASSIUM PHOSPHATE, SODIUM PHOSPHATE, 2-PROPANOL, AMMONIUM CHLORIDE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropMES20 (mM)
31drop100 (mM)
41dropdithiothreitol1 (mM)
51dropEDTA1 (mM)
61reservoir1.0 (M)
71reservoirisopropanol4 (%(v/v))
81reservoirsodium potassium phosphate0.2 (M)
91reservoirPEG335020 (%(w/v))

218853

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