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1QOK

MFE-23 AN ANTI-CARCINOEMBRYONIC ANTIGEN SINGLE-CHAIN FV ANTIBODY

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]291
Detector technologyIMAGE PLATE
Collection date1994-03-15
DetectorR-AXIS II
Spacegroup nameP 32 2 1
Unit cell lengths61.700, 61.700, 128.000
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution8.000 - 2.400
R-factor0.205
Rwork0.205
R-free0.26700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2fbj
RMSD bond length0.010
RMSD bond angle1.700

*

Data reduction softwareDENZO
Data scaling softwareCCP4
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.530
High resolution limit [Å]2.4002.400
Rmerge0.0820.189
Number of reflections115391613

*

<I/σ(I)>4.43.2
Completeness [%]99.6100
Redundancy5.35.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.518

*

CRYSTALS WERE GROWN BY THE HANGING-DROP VAPOUR DIFFUSION METHOD AT 18 DEGREES (CELSIUS). PROTEIN SOLUTION (2 MG/ML) WAS MIXED 1:1 WITH 100 MM TRIS-HCL (PH6.5) CONTAINING 45% SATURATED AMMONIUM SULPHATE. A 10 UL DROPLET OF THIS MIXTURE WAS EQULIBRATED AGAINST 0.5 ML 100 MM TRIS-HCL (PH6.5) IN 45% AMMONIUM SULPHATE., pH 6.50
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein1 (mg/ml)
21dropTris-HCl50 (mM)
31dropammonium sulfate22.5 (%sat)
41reservoirTris-HCl100 (mM)
51reservoirammonium sulfate45 (%sat)

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PDB entries from 2024-05-15

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