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2VXV

Crystal structure of human IgG ABT-325 Fab Fragment

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 32-ID
Synchrotron siteAPS
Beamline32-ID
Temperature [K]100
Detector technologyCCD
Collection date2003-04-29
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths64.406, 74.069, 107.271
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.710 - 1.490
R-factor0.155
Rwork0.153
R-free0.17900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1fns
RMSD bond length0.015
RMSD bond angle1.569
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.540
High resolution limit [Å]1.4901.490
Rmerge0.0800.410
Number of reflections83126
<I/σ(I)>9.83.1
Completeness [%]99.092.3
Redundancy6.44.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
110.5277ABT-325 FAB FRAGMENT (20 MG/ML, 2 MICROLITERS [UL]) WAS MIXED WITH 2 UL OF A RESERVOIR SOLUTION CONSISTING OF 25 TO 30% POLYETHYLENEGLYCOL (PEG) 400, 100 MM CAPS, PH 10.5 AND SUSPENDED OVER THE RESERVOIR AT 277 K. ROD-LIKE CRYSTALS APPEARED WITHIN ONE DAY.

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