X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution.
We have grown crystals in trigonal space group P3(2)21 of a mutant human myoglobin, aquomet form, in which lysine at position 45 has been replaced by arginine and cysteine at position 110 has been replaced by alanine. Suitable crystals of native recombinant human myoglobin have not been obtained. We have used the molecular replacement method to determine the X-ray crystal structure of the mutant at 2.8 A resolution. At the present stage of refinement, the crystallographic R-value for the model, with tightly restrained stereochemistry, is 0.158 for 5.0 to 2.8 A data. As expected, the overall structure is quite similar to the sperm whale myoglobin structure. Arginine 45 adopts a well-ordered conformation similar to that found in aquomet sperm whale myoglobin.
Hubbard
S R
SR
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
Hendrickson
W A
WA
Lambright
D G
DG
Boxer
S G
SG
D006801:Humans; D015394:Molecular Structure; D009154:Mutation; D009211:Myoglobin / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins; D014961:X-Ray Diffraction
D009211:Myoglobin; D011994:Recombinant Proteins