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1MYR

MYROSINASE FROM SINAPIS ALBA

Experimental procedure
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM1A
Synchrotron siteESRF
BeamlineBM1A
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-09
DetectorMARRESEARCH
Spacegroup nameC 2 2 21
Unit cell lengths134.300, 136.400, 80.300
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution17.400 - 1.640
R-factor0.152
Rwork0.152
R-free0.18700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1cbg
RMSD bond length0.022
RMSD bond angle23.800

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]17.4001.730
High resolution limit [Å]1.6401.640
Rmerge0.0650.190
Number of reflections88638
<I/σ(I)>7.72.4
Completeness [%]98.390.7
Redundancy4.63.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.5HANGING DROP METHOD, 12 MG/ML PROTEIN IN 30 MM HEPES, PH 6.5, 0.05 % NAN3 PRECIPITANT 66 % SAT. AMMONIUM SULFATE, 100MM TRIS-HCL, vapor diffusion - hanging drop
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropmyrosinase12 (mg/ml)
21dropHEPES30 (mM)
31drop0.05 (%)
41reservoirammonium sulfate66 (%sat)
51reservoirTris-HCl100 (mM)

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PDB entries from 2024-05-01

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