The structure of one of the basic members of the cell-membrane water-channel family, a protein called aquaporin 1 (AQP1), has been determined to a resolution of 2.2 angstroms (22 billionths of a meter).
The structure reveals the elegantly simple means by which AQP1 can transport water through the cell membrane at a high rate while effectively blocking everything else, even individual protons, the nuclei of hydrogen atoms.
Biophysicist Bing Jap led a team from Lawrence Berkeley National Laboratory’s Life Sciences Division in the difficult and painstaking crystallization of this membrane protein, whose crystal structure was then solved from x-ray diffraction at Beamline 5.0.2 of Berkeley Lab’s Advanced Light Source. Their report appears in the journal Nature today.
Paul Preuss | International Science News
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