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1RQI

Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.3
Synchrotron siteALS
Beamline5.0.3
Temperature [K]97
Detector technologyCCD
Collection date2002-11-11
DetectorADSC QUANTUM 4
Wavelength(s)1.00
Spacegroup nameP 41 2 2
Unit cell lengths88.839, 88.839, 174.769
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000

*

- 2.420
R-factor0.20604
Rwork0.203
R-free0.26000

*

Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.012
RMSD bond angle1.742
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.510
High resolution limit [Å]2.4202.420
Rmerge0.100

*

0.443

*

Total number of observations194920

*

Number of reflections26473
<I/σ(I)>15.93.2
Completeness [%]96.193.2
Redundancy7.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1unknown

*

6298Hosfield, D., (2003) J. Struct. Biol., 142, 207.

*

229380

PDB entries from 2024-12-25

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