Laser-induced optical breakdown by femtosecond pulses is extraordinarily precise when the energy is near threshold. Despite numerous applications, the basis for this deterministic nature has not been determined. We present experiments that shed light on the basic mechanisms of light–matter interactions in this regime, which we term “optics at critical intensity.” We find that the remarkably sharp threshold for laser-induced material damage enables the structure or properties of materials to be modified with nanometer precision. Through detailed study of the minimum ablation size and the effects of polarization, we propose a fundamental framework for describing light–matter interactions in this regime. In surprising contrast to accepted damage theory, multiphoton ionization does not play a significant role. Our results also reject the use of the Keldysh parameter in predicting the role of multiphoton effects. We find that the dominant mechanism is Zener ionization followed by a combination of Zener and Zener-seeded avalanche ionization. We predict that the minimum feature size ultimately depends on the valence electron density, which is sufficiently high and uniform, to confer deterministic behavior on the damage threshold even at the nanoscale. This behavior enables nanomachining with high precision, which we demonstrate by machining highly reproducible nanometer-sized holes and grooves in dielectrics.

When chromosomes are aligned and bioriented at metaphase, the elastic stretch of centromeric chromatin opposes pulling forces exerted on sister kinetochores by the mitotic spindle. Here we show that condensin ATPase activity is an important regulator of centromere stiffness and function. Condensin depletion decreases the stiffness of centromeric chromatin by 50% when pulling forces are applied to kinetochores. However, condensin is dispensable for the normal level of compaction (rest length) of centromeres, which probably depends on other factors that control higher-order chromatin folding. Kinetochores also do not require condensin for their structure or motility. Loss of stiffness caused by condensin-depletion produces abnormal uncoordinated sister kinetochore movements, leads to an increase in Mad2(+) kinetochores near the metaphase plate and delays anaphase onset.

The spindle assembly checkpoint (SAC) is a unique signalling mechanism that responds to the state of attachment of the kinetochore to spindle microtubules. SAC signalling is activated by unattached kinetochores, and it is silenced after these kinetochores form end-on microtubule attachments. Although the biochemical cascade of SAC signalling is well understood, how kinetochore–microtubule attachment disrupts it remained unknown. Here we show that, in budding yeast, end-on microtubule attachment to the kinetochore physically separates the Mps1 kinase, which probably binds to the calponin homology domain of Ndc80, from the kinetochore substrate of Mps1, Spc105 (KNL1 orthologue). This attachment-mediated separation disrupts the phosphorylation of Spc105, and enables SAC silencing. Additionally, the Dam1 complex may act as a barrier that shields Spc105 from Mps1. Together these data suggest that the protein architecture of the kinetochore encodes a mechanical switch. End-on microtubule attachment to the kinetochore turns this switch off to silence the SAC.