Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes.
The 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes has been expressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals were grown using a salting-in technique. Crystals have a tetragonal plate shape and belong to the C2 space group, with unit-cell parameters a = 163.9, b = 106.5, c = 93.5 A, beta = 95.5 degrees. The crystals diffract to 2.8 A resolution.
Han
B G
BG
Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720, USA.
Nunomura
W
W
Wu
H
H
Mohandas
N
N
Jap
B K
BK
D003460:Crystallization; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood* / Q000737:chemistry*; D008970:Molecular Weight; D009479:Neuropeptides; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1