title: A survey of global radiation damage to 15 different protein crystal types at room temperature: a new decay model.
abstract: The radiation damage rates to crystals of 15 model macromolecular structures were studied using an automated radiation sensitivity characterization procedure. The diffracted intensity variation with dose is described by a two-parameter model. This model includes a strong resolution-independent decay specific to room-temperature measurements along with a linear increase in overall Debye-Waller factors. An equivalent representation of sensitivity via a single parameter, normalized half-dose, is introduced. This parameter varies by an order of magnitude between the different structures studied. The data show a correlation of crystal radiation sensitivity with crystal solvent content but no dose-rate dependency was detected in the range 0.05-300 kGy s(-1). The results of the crystal characterization are suitable for either optimal planning of room-temperature data collection or in situ crystallization plate screening experiments.
authors.affiliation: ESRF, BP-220, 38043 Grenoble, France.
authors.forename: Ricardo Miguel Ferraz
authors.initials: RM
authors.lastname: Leal
authors.forename: Gleb
authors.initials: G
authors.lastname: Bourenkov
authors.forename: Silvia
authors.initials: S
authors.lastname: Russi
authors.forename: Alexander N
authors.initials: AN
authors.lastname: Popov
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008956:Models, Chemical; D011506:Proteins / Q000528:radiation effects*; D012997:Solvents; D013696:Temperature
chemical_list: D011506:Proteins; D012997:Solvents