Crystal structure of recombinant human interleukin-4.

@article{Walter1992CrystalSO,
  title={Crystal structure of recombinant human interleukin-4.},
  author={Mark R. Walter and William Joseph James Cook and B G Zhao and Rachel Cameron and Steven E. Ealick and Richard L. Walter and Paul Reichert and Tattanahalli L. Nagabhushan and Paul Phillip Trotta and Charles E. Bugg},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 28},
  pages={
          20371-6
        }
}
The crystal structure of recombinant human interleukin-4 (rhuIL-4) was initially determined at 3.5-A resolution by multiple isomorphous replacement techniques and subsequently refined to a resolution of 2.35 A by simulated annealing. The final crystallographic R-factor, based on all data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths and bond angles in the molecule have root mean square deviations from ideal values of 0.016 A and 2.4 degrees, respectively. The overall… 
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References

SHOWING 1-2 OF 2 REFERENCES
Hematonoietrc Growth Factors in Clinical ADD& and Arai, K.-I
  • FASEB J. 2,
  • 1988
New York cations