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1OL0

Crystal structure of a camelised human VH

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
Collection date2000-10-15
DetectorADSC CCD
Spacegroup nameP 32 2 1
Unit cell lengths75.300, 75.300, 101.780
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution25.200

*

- 1.800
R-factor0.15576
Rwork0.154
R-free0.18020

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1hcv
RMSD bond length0.017

*

RMSD bond angle0.038

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.200

*

1.830
High resolution limit [Å]1.8001.800
Rmerge0.0510.227
Total number of observations69437

*

Number of reflections29910
<I/σ(I)>17.21.5
Completeness [%]94.971.5
Redundancy2.32
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5CRYSTALS GREW FROM 4 MICROLITRE HANGING DROPS FORMED BY MIXING 2 MICROLITERS OF PROTEIN AT A CONCENTRATION OF 5MG/ML WITH 2 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 15-20% (W/V) PEG 8000, 0.4 M AMMONIUM SULPHATE AND 0.1M HEPES AT PH 7.5.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
21reservoirPEG800015-20 (%(w/v))
31reservoirammonium sulfate0.4 (M)
41reservoirHEPES0.1 (M)pH7.5

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PDB entries from 2024-05-15

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