While I agree that this is a major advance, I think calling this the "holy grail" is going too far. Currently there a several ways of doing large screens for crystallization conditions which utilize robots and nanoliter volumes of protein/condition to screen thousands of precipitant mixtures. The two real major stumbling blocks in crystallography are purification of monodisperse, nearly homogeneous protein (with respect to post-translational modifications as well as identity of the protein species) and the real "holy grail" problem, which is ab initio phase determination. Since X-rays cannot be lensed, the Fourier transform of the diffraction pattern (which is the Fourier synthesis of the ordered electrons in the crystal) requires knowing not only the intensities, a trivial task, but also the relative phase angle of each reflection. This is a problem with possible solutions on the order of 6^n, where n is the total number of unique reflections, or about 5-10,000 for an average macromolecular structure at 3 angstrom Bragg spacing, allowing for a +/- accuracy of 30 degrees for each phase angle. Current solutions rely on searching reciprocal space with similar known structures (Molecular Replacement) or several ab initio methods that require one or more heavy element derivatives of native crystals. The first approach only works for crystals where a very similar structure is already known and available to the investigator. The second approach requires further screening for heavy metals that bind in ordered sites in the crystal without significant alteration of the native lattice, then usually a trip to a tunable X-ray source at a synchrotron. This second approach can burn through an astounding number of crystals and investigator time. There are shortcuts such as making the protein with Seleno-methionine instead of methionine (selenium has a usable X-ray edge for phasing, unlike sulfur),but this is normally done after initial purification and crystallization have been optimized. For more reading on the phase problem, I'd recommend either Alexander McPherson or Jan Drenth's excellent introductory textbooks on macromolecular crystallography.
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While I agree that this is a major advance, I think calling this the "holy grail" is going too far. Currently there a several ways of doing large screens for crystallization conditions which utilize robots and nanoliter volumes of protein/condition to screen thousands of precipitant mixtures. The two real major stumbling blocks in crystallography are purification of monodisperse, nearly homogeneous protein (with respect to post-translational modifications as well as identity of the protein species) and the real "holy grail" problem, which is ab initio phase determination.
Since X-rays cannot be lensed, the Fourier transform of the diffraction pattern (which is the Fourier synthesis of the ordered electrons in the crystal) requires knowing not only the intensities, a trivial task, but also the relative phase angle of each reflection. This is a problem with possible solutions on the order of 6^n, where n is the total number of unique reflections, or about 5-10,000 for an average macromolecular structure at 3 angstrom Bragg spacing, allowing for a +/- accuracy of 30 degrees for each phase angle. Current solutions rely on searching reciprocal space with similar known structures (Molecular Replacement) or several ab initio methods that require one or more heavy element derivatives of native crystals. The first approach only works for crystals where a very similar structure is already known and available to the investigator. The second approach requires further screening for heavy metals that bind in ordered sites in the crystal without significant alteration of the native lattice, then usually a trip to a tunable X-ray source at a synchrotron. This second approach can burn through an astounding number of crystals and investigator time. There are shortcuts such as making the protein with Seleno-methionine instead of methionine (selenium has a usable X-ray edge for phasing, unlike sulfur),but this is normally done after initial purification and crystallization have been optimized. For more reading on the phase problem, I'd recommend either Alexander McPherson or Jan Drenth's excellent introductory textbooks on macromolecular crystallography.