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A comparison of hydrogenous and perdeuterated haloalkane dehalogenase shows similar overall structures with only slight alterations in surface regions. However, perdeuteration causes exclusion of a critical water nucleophile from the active site leading to a structure of an inactive, low pH enzyme form.

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The complete structure (including H atoms) of photoactive yellow protein has been determined in D2O-soaked crystals through the application of joint X-ray (1.1 Å) and neutron (2.5 Å) structure refinement in combination with cross-validated maximum-likelihood simulated annealing.
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